SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00918

- CAH2_HUMAN

UniProt

P00918 - CAH2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Carbonic anhydrase 2
Gene
CA2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Essential for bone resorption and osteoclast differentiation By similarity. Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6.3 Publications

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zinc. Can also use cobalt(II) with lower efficiency, but not copper(II), nickel(II) and manganese(II).1 Publication

Enzyme regulationi

Activated by X-ray, histamine, L-adrenaline, L- and D-phenylalanine, L- and D-histidine, L-His-OMe and beta-Ala-His (carnosine). Competitively inhibited by saccharin, thioxolone, coumarins, 667-coumate, celecoxib (Celebrex), valdecoxib (Bextra), SC-125, SC-560, diclofenac, acetate, azide, bromide, sulfonamide derivatives such as acetazolamide (AZA), methazolamide (MZA), ethoxzolamide (EZA), dichlorophenamide (DCP), brinzolamide, dansylamide, thiabendazole-5-sulfonamide, trifluoromethane sulfonamide and N-hydroxysulfamide, fructose-based sugar sulfamate RWJ-37497, and Foscarnet (phosphonoformate trisodium salt). Repressed strongly by hydrogen sulfide(HS) and weakly by nitrate (NO3). Esterase activity weakly reduced by cyanamide. N-hydroxyurea interfers with zinc binding and inhibit activity.27 Publications

Absorptioni

Abs(max)=550 nm10 Publications

At pH 7.0. Shows a second maximum at 618 nm.

Kineticsi

  1. KM=10 mM for CO2
  2. KM=82 mM for H2CO3
  3. KM=3 mM for 4-nitrophenyl acetate

pH dependencei

Optimum pH is 6-8.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621Activator
Active sitei64 – 641
Active sitei67 – 671
Binding sitei67 – 671Activator
Binding sitei92 – 921Activator
Metal bindingi94 – 941Zinc; catalytic1 Publication
Metal bindingi96 – 961Zinc; catalytic
Metal bindingi119 – 1191Zinc; catalytic
Active sitei127 – 1271

GO - Molecular functioni

  1. carbonate dehydratase activity Source: ProtInc
  2. protein binding Source: UniProtKB
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. angiotensin-activated signaling pathway Source: UniProtKB
  2. bicarbonate transport Source: Reactome
  3. carbon dioxide transport Source: Ensembl
  4. kidney development Source: Ensembl
  5. morphogenesis of an epithelium Source: Ensembl
  6. odontogenesis of dentin-containing tooth Source: Ensembl
  7. one-carbon metabolic process Source: InterPro
  8. positive regulation of bone resorption Source: Ensembl
  9. positive regulation of cellular pH reduction Source: Ensembl
  10. positive regulation of dipeptide transmembrane transport Source: UniProtKB
  11. positive regulation of osteoclast differentiation Source: Ensembl
  12. regulation of anion transport Source: UniProtKB
  13. regulation of intracellular pH Source: UniProtKB
  14. response to estrogen Source: Ensembl
  15. response to pH Source: Ensembl
  16. response to zinc ion Source: Ensembl
  17. secretion Source: Ensembl
  18. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 2681.
ReactomeiREACT_121123. Reversible hydration of carbon dioxide.
REACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
SABIO-RKP00918.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 2 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase II
Carbonic anhydrase C
Short name:
CAC
Carbonic anhydrase II
Short name:
CA-II
Gene namesi
Name:CA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:1373. CA2.

Subcellular locationi

Cytoplasm. Cell membrane
Note: Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells.1 Publication

GO - Cellular componenti

  1. apical part of cell Source: UniProtKB
  2. axon Source: Ensembl
  3. basolateral plasma membrane Source: Ensembl
  4. cytoplasm Source: UniProtKB
  5. cytosol Source: Reactome
  6. extracellular space Source: Ensembl
  7. extracellular vesicular exosome Source: UniProt
  8. microvillus Source: Ensembl
  9. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Osteopetrosis, autosomal recessive 3 (OPTB3) [MIM:259730]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921Q → P in OPTB3; in Czechoslovakia. 2 Publications
VAR_001381
Natural varianti94 – 941H → Y in OPTB3; partial loss of activity. 1 Publication
VAR_021009
Natural varianti107 – 1071H → Y in OPTB3; frequent mutation. 4 Publications
VAR_001382
Natural varianti144 – 1441G → R in OPTB3; complete loss of activity. 1 Publication
VAR_021010

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51W → A: Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with W-64. 1 Publication
Mutagenesisi7 – 71Y → F: Enhanced activity. 2 Publications
Mutagenesisi7 – 71Y → H: Reduced proton transfer rate. 2 Publications
Mutagenesisi62 – 621N → A: Reduced activity. 3 Publications
Mutagenesisi62 – 621N → D: Strongly reduced activity. 3 Publications
Mutagenesisi62 – 621N → H: Reduced proton transfer; when associated with A-64. 3 Publications
Mutagenesisi62 – 621N → L: Reduced activity. 3 Publications
Mutagenesisi62 – 621N → T: Reduced activity. 3 Publications
Mutagenesisi62 – 621N → V: Reduced activity. 3 Publications
Mutagenesisi64 – 641H → A: Reduced CO(2) hydrase activity, rescued by 4-methylimidazole (4-MI). Reduced proton transfer; when associated with H-62. Enhanced proton transfer; when associated with H-67. Enhanced proton transfer capacity; when associated with H-99. 4 Publications
Mutagenesisi64 – 641H → G: Impaired activity, not rescued by 4-methylimidazole (4-MI). 4 Publications
Mutagenesisi64 – 641H → W: Impaired activity, rescued by 4-methylimidazole (4-MI). Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with A-5. 4 Publications
Mutagenesisi65 – 651A → F: Reduced activity. 1 Publication
Mutagenesisi65 – 651A → H, L or S: Normal activity. 1 Publication
Mutagenesisi67 – 671N → H: Enhanced proton transfer; when associated with A-64. 3 Publications
Mutagenesisi67 – 671N → L: Reduced activity. 3 Publications
Mutagenesisi67 – 671N → Q: Normal activity. 3 Publications
Mutagenesisi94 – 941H → C, D, E, N or Q: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities, impaired stability of zinc binding. 2 Publications
Mutagenesisi106 – 1061E → A or Q: Strongly reduced CO(2) hydrase activity. 2 Publications
Mutagenesisi106 – 1061E → D: Normal CO(2) hydrase activity. 2 Publications
Mutagenesisi117 – 1171E → Q: Strongly reduced activity and sulfonamide affinity. 1 Publication
Mutagenesisi119 – 1191H → D, N or Q: Reduced activity. 1 Publication
Mutagenesisi119 – 1191H → E: Strongly reduced activity. 1 Publication
Mutagenesisi121 – 1211V → A, G, I, L or S: Reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. 1 Publication
Mutagenesisi121 – 1211V → K or R: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. 1 Publication
Mutagenesisi142 – 1421V → F or Y: Strongly impaired activity. 1 Publication
Mutagenesisi142 – 1421V → G: Weakly impaired activity. 1 Publication
Mutagenesisi142 – 1421V → H: Impaired activity. 1 Publication
Mutagenesisi197 – 1971L → A: Reduced CO(2) hydrase activity. 1 Publication
Mutagenesisi197 – 1971L → E, H or R: Strongly reduced CO(2) hydrase activity. 1 Publication
Mutagenesisi197 – 1971L → F: Normal activity. 1 Publication
Mutagenesisi198 – 1981T → A, C, H or P: Strongly reduced activity. 5 Publications
Mutagenesisi198 – 1981T → D or E: Strongly reduced activity, but enhanced zinc affinity. 5 Publications
Mutagenesisi198 – 1981T → S or V: Reduced activity. 5 Publications
Mutagenesisi199 – 1991T → H: Higher affinity for bicarbonate. Enhanced proton transfer capacity; when associated with A-64. 3 Publications
Mutagenesisi199 – 1991T → S: Enhanced p-nitrophenyl acetate esterase activity, but normal CO(2) hydrase activity. 3 Publications
Mutagenesisi201 – 2011P → A: Normal CO(2) hydrase activity, but impaired stability. 1 Publication

Keywords - Diseasei

Disease mutation, Osteopetrosis

Organism-specific databases

MIMi259730. phenotype.
Orphaneti2785. Osteopetrosis with renal tubular acidosis.
PharmGKBiPA25989.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 260259Carbonic anhydrase 2
PRO_0000077418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP00918.
PaxDbiP00918.
PeptideAtlasiP00918.
PRIDEiP00918.

2D gel databases

OGPiP00918.
REPRODUCTION-2DPAGEIPI00218414.
P00918.
UCD-2DPAGEP00918.

PTM databases

PhosphoSiteiP00918.

Expressioni

Gene expression databases

ArrayExpressiP00918.
BgeeiP00918.
CleanExiHS_CA2.
GenevestigatoriP00918.

Organism-specific databases

HPAiCAB010102.
HPA001550.

Interactioni

Subunit structurei

Interacts with SLC4A4. Interaction with SLC4A7 regulates SLC4A7 transporter activity. Interacts with SLC26A6 isoform 4 (via C-terminus cytoplasmic domain).4 Publications

Protein-protein interaction databases

BioGridi107215. 12 interactions.
IntActiP00918. 5 interactions.
MINTiMINT-1367766.
STRINGi9606.ENSP00000285379.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni9 – 113
Turni13 – 153
Helixi16 – 183
Helixi21 – 244
Beta strandi25 – 273
Beta strandi31 – 333
Turni35 – 373
Beta strandi38 – 403
Beta strandi42 – 443
Beta strandi45 – 506
Beta strandi56 – 616
Beta strandi63 – 708
Beta strandi73 – 753
Beta strandi77 – 826
Beta strandi88 – 9710
Beta strandi106 – 1094
Beta strandi115 – 12410
Helixi125 – 1273
Helixi130 – 1334
Beta strandi139 – 15113
Helixi154 – 1563
Helixi157 – 1626
Helixi163 – 1653
Beta strandi172 – 1743
Helixi180 – 1834
Beta strandi190 – 1956
Beta strandi206 – 2138
Beta strandi215 – 2173
Helixi219 – 2257
Beta strandi229 – 2313
Beta strandi233 – 2353
Beta strandi256 – 2583

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
12CAX-ray2.40A1-260[»]
1A42X-ray2.25A2-260[»]
1AM6X-ray2.00A2-260[»]
1AVNX-ray2.00A2-260[»]
1BCDX-ray1.90A2-260[»]
1BICX-ray1.90A2-260[»]
1BN1X-ray2.10A2-260[»]
1BN3X-ray2.20A2-260[»]
1BN4X-ray2.10A2-260[»]
1BNMX-ray2.60A2-260[»]
1BNNX-ray2.30A2-260[»]
1BNQX-ray2.40A2-260[»]
1BNTX-ray2.15A2-260[»]
1BNUX-ray2.15A2-260[»]
1BNVX-ray2.40A2-260[»]
1BNWX-ray2.25A2-260[»]
1BV3X-ray1.85A2-260[»]
1CA2X-ray2.00A2-260[»]
1CA3X-ray2.30A1-260[»]
1CAHX-ray1.88A2-260[»]
1CAIX-ray1.80A2-260[»]
1CAJX-ray1.90A2-260[»]
1CAKX-ray1.90A2-260[»]
1CALX-ray2.20A2-260[»]
1CAMX-ray1.70A2-260[»]
1CANX-ray1.90A2-260[»]
1CAOX-ray1.90A2-260[»]
1CAYX-ray2.10A2-260[»]
1CAZX-ray1.90A2-260[»]
1CCSX-ray2.35A2-260[»]
1CCTX-ray2.20A2-260[»]
1CCUX-ray2.25A2-260[»]
1CILX-ray1.60A2-260[»]
1CIMX-ray2.10A2-260[»]
1CINX-ray2.10A2-260[»]
1CNBX-ray2.35A2-260[»]
1CNCX-ray2.20A2-260[»]
1CNGX-ray1.90A2-260[»]
1CNHX-ray2.05A2-260[»]
1CNIX-ray1.80A2-260[»]
1CNJX-ray1.80A2-260[»]
1CNKX-ray2.15A2-260[»]
1CNWX-ray2.00A1-260[»]
1CNXX-ray1.90A1-260[»]
1CNYX-ray2.30A1-260[»]
1CRAX-ray1.90A2-260[»]
1CVAX-ray2.25A2-260[»]
1CVBX-ray2.40A2-260[»]
1CVCX-ray2.30A2-260[»]
1CVDX-ray2.20A5-259[»]
1CVEX-ray2.25A2-260[»]
1CVFX-ray2.25A2-260[»]
1CVHX-ray2.30A5-259[»]
1DCAX-ray2.20A1-260[»]
1DCBX-ray2.10A1-260[»]
1EOUX-ray2.10A1-260[»]
1F2WX-ray1.90A2-260[»]
1FQLX-ray2.00A1-260[»]
1FQMX-ray2.00A1-260[»]
1FQNX-ray2.00A1-260[»]
1FQRX-ray2.00A1-260[»]
1FR4X-ray1.60A1-260[»]
1FR7X-ray1.50A/B1-260[»]
1FSNX-ray2.00A/B1-260[»]
1FSQX-ray2.00A/B1-260[»]
1FSRX-ray2.00A/B1-260[»]
1G0EX-ray1.60A1-260[»]
1G0FX-ray1.60A1-260[»]
1G1DX-ray2.04A2-260[»]
1G3ZX-ray1.86A2-260[»]
1G45X-ray1.83A2-260[»]
1G46X-ray1.84A2-260[»]
1G48X-ray1.86A2-260[»]
1G4JX-ray1.84A2-260[»]
1G4OX-ray1.96A2-260[»]
1G52X-ray1.80A2-260[»]
1G53X-ray1.94A2-260[»]
1G54X-ray1.86A2-260[»]
1H4NX-ray2.00A2-260[»]
1H9NX-ray1.85A2-260[»]
1H9QX-ray2.20A2-260[»]
1HCAX-ray2.30A1-260[»]
1HEAX-ray2.00A1-260[»]
1HEBX-ray2.00A1-260[»]
1HECX-ray2.00A1-260[»]
1HEDX-ray2.00A1-260[»]
1HVAX-ray2.30A1-260[»]
1I8ZX-ray1.93A2-260[»]
1I90X-ray2.00A2-260[»]
1I91X-ray2.00A2-260[»]
1I9LX-ray1.93A2-260[»]
1I9MX-ray1.84A2-260[»]
1I9NX-ray1.86A2-260[»]
1I9OX-ray1.86A2-260[»]
1I9PX-ray1.92A2-260[»]
1I9QX-ray1.80A2-260[»]
1IF4X-ray1.93A2-260[»]
1IF5X-ray2.00A2-260[»]
1IF6X-ray2.09A2-259[»]
1IF7X-ray1.98A2-260[»]
1IF8X-ray1.94A2-260[»]
1IF9X-ray2.00A2-260[»]
1KWQX-ray2.60A1-260[»]
1KWRX-ray2.25A1-260[»]
1LG5X-ray1.75A1-260[»]
1LG6X-ray2.20A1-260[»]
1LGDX-ray1.90A1-260[»]
1LUGX-ray0.95A2-260[»]
1LZVX-ray2.30A1-260[»]
1MOOX-ray1.05A1-260[»]
1MUAX-ray1.70A4-259[»]
1OKLX-ray2.10A2-260[»]
1OKMX-ray2.20A2-260[»]
1OKNX-ray2.40A2-260[»]
1OQ5X-ray1.50A2-259[»]
1RAYX-ray1.80A2-260[»]
1RAZX-ray1.90A2-260[»]
1RZAX-ray1.90A2-260[»]
1RZBX-ray1.80A2-260[»]
1RZCX-ray1.90A2-260[»]
1RZDX-ray1.90A2-260[»]
1RZEX-ray1.90A2-260[»]
1T9NX-ray2.00A1-259[»]
1TB0X-ray2.00X1-259[»]
1TBTX-ray2.00X1-259[»]
1TE3X-ray2.00X1-260[»]
1TEQX-ray2.00X1-260[»]
1TEUX-ray2.00X1-260[»]
1TG3X-ray1.80A1-260[»]
1TG9X-ray1.90A1-260[»]
1TH9X-ray1.63A1-260[»]
1THKX-ray1.80A1-260[»]
1TTMX-ray1.95A2-259[»]
1UGAX-ray2.00A3-260[»]
1UGBX-ray2.00A3-260[»]
1UGCX-ray2.00A3-260[»]
1UGDX-ray2.00A3-260[»]
1UGEX-ray1.90A3-260[»]
1UGFX-ray2.00A3-260[»]
1UGGX-ray2.20A3-260[»]
1XEGX-ray1.81A1-260[»]
1XEVX-ray2.20A/B/C/D1-260[»]
1XPZX-ray2.02A3-260[»]
1XQ0X-ray1.76A2-260[»]
1YDAX-ray2.10A2-260[»]
1YDBX-ray1.90A2-260[»]
1YDCX-ray1.95A2-260[»]
1YDDX-ray2.10A2-260[»]
1YO0X-ray1.80A1-260[»]
1YO1X-ray1.70A1-260[»]
1YO2X-ray1.80A1-259[»]
1Z9YX-ray1.66A2-259[»]
1ZE8X-ray2.00A2-260[»]
1ZFKX-ray1.56A2-259[»]
1ZFQX-ray1.55A2-259[»]
1ZGEX-ray1.65A2-259[»]
1ZGFX-ray1.75A2-259[»]
1ZH9X-ray1.70A2-259[»]
1ZSAX-ray2.50A2-260[»]
1ZSBX-ray2.00A2-260[»]
1ZSCX-ray1.80A2-260[»]
2ABEX-ray2.00A2-259[»]
2AW1X-ray1.46A2-260[»]
2AX2X-ray1.50A1-259[»]
2CA2X-ray1.90A2-260[»]
2CBAX-ray1.54A2-260[»]
2CBBX-ray1.67A2-260[»]
2CBCX-ray1.88A2-260[»]
2CBDX-ray1.67A2-260[»]
2CBEX-ray1.82A2-260[»]
2EU2X-ray1.15A1-260[»]
2EU3X-ray1.60A1-260[»]
2EZ7X-ray2.00A1-259[»]
2F14X-ray1.71A2-259[»]
2FMGX-ray1.60A1-259[»]
2FMZX-ray1.60A1-259[»]
2FNKX-ray1.80A1-260[»]
2FNMX-ray1.80A1-260[»]
2FNNX-ray1.80A1-260[»]
2FOQX-ray1.25A1-259[»]
2FOSX-ray1.10A1-259[»]
2FOUX-ray0.99A1-259[»]
2FOVX-ray1.15A1-259[»]
2GD8X-ray1.46A2-259[»]
2GEHX-ray2.00A1-259[»]
2H15X-ray1.90A1-259[»]
2H4NX-ray1.90A2-260[»]
2HD6X-ray1.80A2-259[»]
2HKKX-ray1.90A1-260[»]
2HL4X-ray1.55A2-260[»]
2HNCX-ray1.55A2-259[»]
2HOCX-ray2.10A2-259[»]
2ILIX-ray1.05A2-259[»]
2NNGX-ray1.20A2-260[»]
2NNOX-ray1.01A2-260[»]
2NNSX-ray1.03A2-260[»]
2NNVX-ray1.10A2-260[»]
2NWOX-ray1.70A1-259[»]
2NWPX-ray1.80A1-259[»]
2NWYX-ray1.65A1-259[»]
2NWZX-ray1.80A1-259[»]
2NXRX-ray1.70A1-259[»]
2NXSX-ray1.80A1-259[»]
2NXTX-ray1.15A1-260[»]
2O4ZX-ray2.10A1-260[»]
2OSFX-ray1.60A2-260[»]
2OSMX-ray1.60A2-260[»]
2POUX-ray1.60A1-259[»]
2POVX-ray1.60A1-258[»]
2POWX-ray1.75A1-259[»]
2Q1BX-ray1.70A1-260[»]
2Q1QX-ray1.90A1-260[»]
2Q38X-ray1.95A1-260[»]
2QO8X-ray1.40A2-260[»]
2QOAX-ray1.60A2-260[»]
2QP6X-ray1.45A2-260[»]
2VVAX-ray1.56X1-260[»]
2VVBX-ray1.66X1-260[»]
2WD2X-ray1.49A2-259[»]
2WD3X-ray1.80A2-260[»]
2WEGX-ray1.10A2-260[»]
2WEHX-ray2.09A2-260[»]
2WEJX-ray1.45A2-260[»]
2WEOX-ray1.40A2-260[»]
2X7SX-ray1.64A2-260[»]
2X7TX-ray1.89A2-260[»]
2X7UX-ray2.12A2-260[»]
3B4FX-ray1.89A1-260[»]
3BETX-ray1.85A2-260[»]
3BL0X-ray1.90A1-260[»]
3BL1X-ray2.10A1-260[»]
3C7PX-ray1.70A1-260[»]
3CA2X-ray2.00A2-260[»]
3CAJX-ray1.80A1-260[»]
3CYUX-ray1.70A1-260[»]
3D8WX-ray1.70A1-260[»]
3D92X-ray1.10A1-260[»]
3D93X-ray1.10A1-260[»]
3D9ZX-ray1.65A1-260[»]
3DAZX-ray1.60A1-260[»]
3DBUX-ray1.70A1-260[»]
3DC3X-ray1.70A1-260[»]
3DC9X-ray1.60A1-260[»]
3DCCX-ray1.60A1-260[»]
3DCSX-ray1.80A1-260[»]
3DCWX-ray1.50A1-260[»]
3DD0X-ray1.48A1-260[»]
3DD8X-ray1.90A1-260[»]
3DV7X-ray1.70A2-260[»]
3DVBX-ray1.70A2-260[»]
3DVCX-ray1.60A2-260[»]
3DVDX-ray1.60A2-260[»]
3EFIX-ray1.75A2-260[»]
3EFTX-ray1.85A1-260[»]
3F4XX-ray1.90A1-260[»]
3F8EX-ray2.00A1-260[»]
3FFPX-ray1.81X1-260[»]
3GZ0X-ray1.26A2-260[»]
3HFPX-ray2.10A1-260[»]
3HKNX-ray1.80A1-260[»]
3HKQX-ray1.70A1-260[»]
3HKTX-ray2.36A1-260[»]
3HKUX-ray1.80A1-260[»]
3HLJX-ray1.44A1-260[»]
3HS4X-ray1.10A1-260[»]
3IBIX-ray1.93A2-260[»]
3IBLX-ray1.55A2-260[»]
3IBNX-ray2.20A2-260[»]
3IBUX-ray1.41A2-260[»]
3IEOX-ray2.00A1-260[»]
3IGPX-ray1.65A1-260[»]
3K2FX-ray1.98A1-260[»]
3K34X-ray0.90A1-260[»]
3K7KX-ray1.90A1-260[»]
3KIGX-ray1.39A1-260[»]
3KKXneutron diffraction2.00A1-260[»]
3KNEX-ray1.35A1-260[»]
3KOIX-ray1.64A1-260[»]
3KOKX-ray1.50A1-260[»]
3KONX-ray1.50A1-260[»]
3KS3X-ray0.90A1-260[»]
3KWAX-ray2.00A1-260[»]
3L14X-ray1.22A1-260[»]
3M04X-ray1.40A1-260[»]
3M14X-ray1.38A1-260[»]
3M1JX-ray1.80A1-260[»]
3M1KX-ray1.35A1-260[»]
3M1QX-ray1.69A1-260[»]
3M1WX-ray1.38A1-260[»]
3M2NX-ray1.65A1-260[»]
3M2XX-ray1.87A1-260[»]
3M2YX-ray1.17A1-260[»]
3M2ZX-ray1.70A1-260[»]
3M3XX-ray1.68A1-260[»]
3M40X-ray1.60A1-260[»]
3M5EX-ray1.70A1-260[»]
3M5SX-ray1.40A1-260[»]
3M5TX-ray1.95A1-260[»]
3M67X-ray1.80A1-260[»]
3M96X-ray1.40A1-260[»]
3M98X-ray1.50A1-260[»]
3MHCX-ray1.70A1-260[»]
3MHIX-ray1.70A1-260[»]
3MHLX-ray1.90A1-260[»]
3MHMX-ray1.50A1-260[»]
3MHOX-ray1.15A1-260[»]
3ML2X-ray1.80A1-260[»]
3MMFX-ray1.50A1-260[»]
3MNAX-ray1.50A1-260[»]
3MNHX-ray1.65A1-260[»]
3MNIX-ray1.75A1-260[»]
3MNJX-ray1.75A1-260[»]
3MNKX-ray1.75A1-260[»]
3MNUX-ray1.80A2-260[»]
3MWOX-ray1.40A/B1-260[»]
3MYQX-ray1.35A1-260[»]
3MZCX-ray1.50A1-260[»]
3N0NX-ray1.50A1-260[»]
3N2PX-ray1.65A1-260[»]
3N3JX-ray1.50A1-260[»]
3N4BX-ray1.60A1-260[»]
3NB5X-ray1.80A1-260[»]
3NI5X-ray2.10A1-260[»]
3NJ9X-ray2.00A1-260[»]
3OIKX-ray1.50A1-260[»]
3OILX-ray1.50A1-260[»]
3OIMX-ray1.45A1-260[»]
3OKUX-ray1.45A1-260[»]
3OKVX-ray1.45A1-260[»]
3OY0X-ray1.60A1-260[»]
3OYQX-ray1.47A1-260[»]
3OYSX-ray1.54A1-260[»]
3P3HX-ray1.50A1-260[»]
3P3JX-ray1.60A1-260[»]
3P44X-ray2.20A1-260[»]
3P4VX-ray2.00A1-260[»]
3P55X-ray2.00A1-260[»]
3P58X-ray1.49A1-260[»]
3P5AX-ray1.49A1-260[»]
3P5LX-ray1.50A1-260[»]
3PJJX-ray1.80A2-260[»]
3PO6X-ray1.47A2-260[»]
3PYKX-ray1.30A1-260[»]
3QYKX-ray1.47A1-260[»]
3R16X-ray1.60A4-260[»]
3R17X-ray1.70B4-260[»]
3RG3X-ray1.90A1-260[»]
3RG4X-ray1.50A1-260[»]
3RGEX-ray2.10A1-260[»]
3RJ7X-ray1.20A3-260[»]
3RLDX-ray1.50A1-260[»]
3RYJX-ray1.39B2-260[»]
3RYVX-ray1.20B2-260[»]
3RYXX-ray1.60B2-260[»]
3RYYX-ray1.16A2-260[»]
3RYZX-ray1.37A2-260[»]
3RZ0X-ray1.80B2-260[»]
3RZ1X-ray1.51B2-260[»]
3RZ5X-ray1.65A2-260[»]
3RZ7X-ray1.80A2-260[»]
3RZ8X-ray1.70A2-260[»]
3S71X-ray1.25B3-260[»]
3S72X-ray1.60B3-260[»]
3S73X-ray1.75B3-260[»]
3S74X-ray1.40B3-260[»]
3S75X-ray1.50B3-260[»]
3S76X-ray1.60A3-260[»]
3S77X-ray1.86B3-260[»]
3S78X-ray1.98B3-260[»]
3S8XX-ray1.30A1-260[»]
3S9TX-ray1.30A1-260[»]
3SAPX-ray1.75A1-260[»]
3SAXX-ray1.10A1-260[»]
3SBHX-ray1.65A1-260[»]
3SBIX-ray1.40A1-260[»]
3T5UX-ray1.75A2-260[»]
3T5ZX-ray1.65A2-260[»]
3T82X-ray2.00A1-260[»]
3T83X-ray1.80A1-260[»]
3T84X-ray2.00A1-260[»]
3T85X-ray2.40A1-260[»]
3TMJOther2.00A3-260[»]
3TVNX-ray1.50X3-260[»]
3TVOX-ray1.60X3-260[»]
3U3AX-ray1.55X1-260[»]
3U45X-ray1.70X1-260[»]
3U47X-ray1.60A1-260[»]
3U7CX-ray0.93A1-260[»]
3V2JX-ray1.70A1-260[»]
3V2MX-ray1.47A1-260[»]
3V3FX-ray2.00A1-260[»]
3V3GX-ray1.56B1-260[»]
3V3HX-ray1.85B1-260[»]
3V3IX-ray1.73B1-260[»]
3V3JX-ray1.63A1-260[»]
3V5GX-ray1.50A1-260[»]
3V7XX-ray1.03A2-260[»]
3VBDX-ray1.05A2-260[»]
3ZP9X-ray1.31A1-260[»]
4BCWX-ray1.50A4-260[»]
4BF1X-ray1.35A2-260[»]
4BF6X-ray1.82A2-260[»]
4CA2X-ray2.10A1-260[»]
4CACX-ray2.20A2-260[»]
4CQ0X-ray1.45A1-260[»]
4DZ7X-ray1.49A1-260[»]
4DZ9X-ray1.49A1-260[»]
4E3DX-ray1.60A1-260[»]
4E3FX-ray1.50A1-260[»]
4E3GX-ray1.55A1-260[»]
4E3HX-ray1.50A1-260[»]
4E49X-ray1.45A1-260[»]
4E4AX-ray1.45A1-260[»]
4E5QX-ray1.70A1-260[»]
4FIKX-ray1.20A1-260[»]
4FL7X-ray1.85A2-260[»]
4FPTX-ray0.98A1-260[»]
4FRCX-ray0.98A1-260[»]
4FU5X-ray0.98A1-260[»]
4FVNX-ray1.05A1-260[»]
4FVOX-ray1.05A1-260[»]
4G0Cneutron diffraction2.00A4-260[»]
4GGEX-ray1.47A1-260[»]
4GL1X-ray1.50X1-260[»]
4HBAX-ray1.76A1-260[»]
4HEWX-ray1.70A1-260[»]
4HEYX-ray1.45A1-260[»]
4HEZX-ray1.34A1-260[»]
4HF3X-ray1.15A1-260[»]
4HT0X-ray1.60A1-260[»]
4IDRX-ray1.60X3-260[»]
4ILXX-ray1.60A4-260[»]
4ITOX-ray1.16A1-260[»]
4ITPX-ray1.70A4-260[»]
4IWZX-ray1.60A4-260[»]
4JS6X-ray1.55A1-260[»]
4JSAX-ray1.50A1-260[»]
4JSSX-ray1.50A1-260[»]
4JSWX-ray1.90A1-260[»]
4JSZX-ray1.90A1-260[»]
4K0SX-ray1.80A4-260[»]
4K0TX-ray1.78A4-260[»]
4K0ZX-ray1.80A3-260[»]
4K13X-ray1.60A4-260[»]
4K1QX-ray1.70A3-260[»]
4KAPX-ray1.45A5-260[»]
4KNIX-ray1.80A1-260[»]
4KNJX-ray2.00A1-260[»]
4L5UX-ray2.05A1-260[»]
4L5VX-ray1.63A1-260[»]
4L5WX-ray1.70A1-260[»]
4LP6X-ray2.15A/B1-260[»]
4M2RX-ray1.99A4-260[»]
4M2UX-ray2.00A4-260[»]
4M2VX-ray1.72A4-260[»]
4M2WX-ray1.66A4-260[»]
4MDGX-ray1.35A3-260[»]
4MDLX-ray1.52A3-260[»]
4MDMX-ray1.55A3-260[»]
4MO8X-ray1.85A1-260[»]
4MTYX-ray1.00A1-260[»]
4N0XX-ray1.63B1-260[»]
4N16X-ray1.54A1-260[»]
5CA2X-ray2.10A1-260[»]
5CACX-ray2.20A2-260[»]
6CA2X-ray2.50A1-260[»]
7CA2X-ray2.40A1-260[»]
8CA2X-ray2.40A1-260[»]
9CA2X-ray2.80A1-260[»]
ProteinModelPortaliP00918.
SMRiP00918. Positions 3-260.

Miscellaneous databases

EvolutionaryTraceiP00918.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 1992Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3338.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP00918.
KOiK18245.
OMAiCFNAENE.
OrthoDBiEOG7WMCK7.
PhylomeDBiP00918.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018443. CA2.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF90. PTHR18952:SF90. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00918-1 [UniParc]FASTAAdd to Basket

« Hide

MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS    50
YDQATSLRIL NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL 100
DGQGSEHTVD KKKYAAELHL VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG 150
SAKPGLQKVV DVLDSIKTKG KSADFTNFDP RGLLPESLDY WTYPGSLTTP 200
PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM VDNWRPAQPL 250
KNRQIKASFK 260
Length:260
Mass (Da):29,246
Last modified:January 23, 2007 - v2
Checksum:i2EC2BB7548F10558
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181K → E in Jogjakarta. 1 Publication
VAR_001380
Natural varianti92 – 921Q → P in OPTB3; in Czechoslovakia. 2 Publications
VAR_001381
Natural varianti94 – 941H → Y in OPTB3; partial loss of activity. 1 Publication
VAR_021009
Natural varianti107 – 1071H → Y in OPTB3; frequent mutation. 4 Publications
VAR_001382
Natural varianti144 – 1441G → R in OPTB3; complete loss of activity. 1 Publication
VAR_021010
Natural varianti236 – 2361P → H in Melbourne. 1 Publication
VAR_001383
Natural varianti252 – 2521N → D.
Corresponds to variant rs2228063 [ dbSNP | Ensembl ].
VAR_001384

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1802DP → AA in AAH11949. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77181
, M77176, M77177, M77178, M77179, M77180 Genomic DNA. Translation: AAA51909.1.
Y00339 mRNA. Translation: CAA68426.1.
X03251 Genomic DNA. Translation: CAA27012.1.
J03037 mRNA. Translation: AAA51908.1.
CR536526 mRNA. Translation: CAG38763.1.
CR541875 mRNA. Translation: CAG46673.1.
AK312978 mRNA. Translation: BAG35815.1.
CH471068 Genomic DNA. Translation: EAW87136.1.
BC011949 mRNA. Translation: AAH11949.1.
M36532 mRNA. Translation: AAA51911.1.
CCDSiCCDS6239.1.
PIRiA27175. CRHU2.
RefSeqiNP_000058.1. NM_000067.2.
UniGeneiHs.155097.

Genome annotation databases

EnsembliENST00000285379; ENSP00000285379; ENSG00000104267.
GeneIDi760.
KEGGihsa:760.
UCSCiuc003ydk.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77181
, M77176 , M77177 , M77178 , M77179 , M77180 Genomic DNA. Translation: AAA51909.1 .
Y00339 mRNA. Translation: CAA68426.1 .
X03251 Genomic DNA. Translation: CAA27012.1 .
J03037 mRNA. Translation: AAA51908.1 .
CR536526 mRNA. Translation: CAG38763.1 .
CR541875 mRNA. Translation: CAG46673.1 .
AK312978 mRNA. Translation: BAG35815.1 .
CH471068 Genomic DNA. Translation: EAW87136.1 .
BC011949 mRNA. Translation: AAH11949.1 .
M36532 mRNA. Translation: AAA51911.1 .
CCDSi CCDS6239.1.
PIRi A27175. CRHU2.
RefSeqi NP_000058.1. NM_000067.2.
UniGenei Hs.155097.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
12CA X-ray 2.40 A 1-260 [» ]
1A42 X-ray 2.25 A 2-260 [» ]
1AM6 X-ray 2.00 A 2-260 [» ]
1AVN X-ray 2.00 A 2-260 [» ]
1BCD X-ray 1.90 A 2-260 [» ]
1BIC X-ray 1.90 A 2-260 [» ]
1BN1 X-ray 2.10 A 2-260 [» ]
1BN3 X-ray 2.20 A 2-260 [» ]
1BN4 X-ray 2.10 A 2-260 [» ]
1BNM X-ray 2.60 A 2-260 [» ]
1BNN X-ray 2.30 A 2-260 [» ]
1BNQ X-ray 2.40 A 2-260 [» ]
1BNT X-ray 2.15 A 2-260 [» ]
1BNU X-ray 2.15 A 2-260 [» ]
1BNV X-ray 2.40 A 2-260 [» ]
1BNW X-ray 2.25 A 2-260 [» ]
1BV3 X-ray 1.85 A 2-260 [» ]
1CA2 X-ray 2.00 A 2-260 [» ]
1CA3 X-ray 2.30 A 1-260 [» ]
1CAH X-ray 1.88 A 2-260 [» ]
1CAI X-ray 1.80 A 2-260 [» ]
1CAJ X-ray 1.90 A 2-260 [» ]
1CAK X-ray 1.90 A 2-260 [» ]
1CAL X-ray 2.20 A 2-260 [» ]
1CAM X-ray 1.70 A 2-260 [» ]
1CAN X-ray 1.90 A 2-260 [» ]
1CAO X-ray 1.90 A 2-260 [» ]
1CAY X-ray 2.10 A 2-260 [» ]
1CAZ X-ray 1.90 A 2-260 [» ]
1CCS X-ray 2.35 A 2-260 [» ]
1CCT X-ray 2.20 A 2-260 [» ]
1CCU X-ray 2.25 A 2-260 [» ]
1CIL X-ray 1.60 A 2-260 [» ]
1CIM X-ray 2.10 A 2-260 [» ]
1CIN X-ray 2.10 A 2-260 [» ]
1CNB X-ray 2.35 A 2-260 [» ]
1CNC X-ray 2.20 A 2-260 [» ]
1CNG X-ray 1.90 A 2-260 [» ]
1CNH X-ray 2.05 A 2-260 [» ]
1CNI X-ray 1.80 A 2-260 [» ]
1CNJ X-ray 1.80 A 2-260 [» ]
1CNK X-ray 2.15 A 2-260 [» ]
1CNW X-ray 2.00 A 1-260 [» ]
1CNX X-ray 1.90 A 1-260 [» ]
1CNY X-ray 2.30 A 1-260 [» ]
1CRA X-ray 1.90 A 2-260 [» ]
1CVA X-ray 2.25 A 2-260 [» ]
1CVB X-ray 2.40 A 2-260 [» ]
1CVC X-ray 2.30 A 2-260 [» ]
1CVD X-ray 2.20 A 5-259 [» ]
1CVE X-ray 2.25 A 2-260 [» ]
1CVF X-ray 2.25 A 2-260 [» ]
1CVH X-ray 2.30 A 5-259 [» ]
1DCA X-ray 2.20 A 1-260 [» ]
1DCB X-ray 2.10 A 1-260 [» ]
1EOU X-ray 2.10 A 1-260 [» ]
1F2W X-ray 1.90 A 2-260 [» ]
1FQL X-ray 2.00 A 1-260 [» ]
1FQM X-ray 2.00 A 1-260 [» ]
1FQN X-ray 2.00 A 1-260 [» ]
1FQR X-ray 2.00 A 1-260 [» ]
1FR4 X-ray 1.60 A 1-260 [» ]
1FR7 X-ray 1.50 A/B 1-260 [» ]
1FSN X-ray 2.00 A/B 1-260 [» ]
1FSQ X-ray 2.00 A/B 1-260 [» ]
1FSR X-ray 2.00 A/B 1-260 [» ]
1G0E X-ray 1.60 A 1-260 [» ]
1G0F X-ray 1.60 A 1-260 [» ]
1G1D X-ray 2.04 A 2-260 [» ]
1G3Z X-ray 1.86 A 2-260 [» ]
1G45 X-ray 1.83 A 2-260 [» ]
1G46 X-ray 1.84 A 2-260 [» ]
1G48 X-ray 1.86 A 2-260 [» ]
1G4J X-ray 1.84 A 2-260 [» ]
1G4O X-ray 1.96 A 2-260 [» ]
1G52 X-ray 1.80 A 2-260 [» ]
1G53 X-ray 1.94 A 2-260 [» ]
1G54 X-ray 1.86 A 2-260 [» ]
1H4N X-ray 2.00 A 2-260 [» ]
1H9N X-ray 1.85 A 2-260 [» ]
1H9Q X-ray 2.20 A 2-260 [» ]
1HCA X-ray 2.30 A 1-260 [» ]
1HEA X-ray 2.00 A 1-260 [» ]
1HEB X-ray 2.00 A 1-260 [» ]
1HEC X-ray 2.00 A 1-260 [» ]
1HED X-ray 2.00 A 1-260 [» ]
1HVA X-ray 2.30 A 1-260 [» ]
1I8Z X-ray 1.93 A 2-260 [» ]
1I90 X-ray 2.00 A 2-260 [» ]
1I91 X-ray 2.00 A 2-260 [» ]
1I9L X-ray 1.93 A 2-260 [» ]
1I9M X-ray 1.84 A 2-260 [» ]
1I9N X-ray 1.86 A 2-260 [» ]
1I9O X-ray 1.86 A 2-260 [» ]
1I9P X-ray 1.92 A 2-260 [» ]
1I9Q X-ray 1.80 A 2-260 [» ]
1IF4 X-ray 1.93 A 2-260 [» ]
1IF5 X-ray 2.00 A 2-260 [» ]
1IF6 X-ray 2.09 A 2-259 [» ]
1IF7 X-ray 1.98 A 2-260 [» ]
1IF8 X-ray 1.94 A 2-260 [» ]
1IF9 X-ray 2.00 A 2-260 [» ]
1KWQ X-ray 2.60 A 1-260 [» ]
1KWR X-ray 2.25 A 1-260 [» ]
1LG5 X-ray 1.75 A 1-260 [» ]
1LG6 X-ray 2.20 A 1-260 [» ]
1LGD X-ray 1.90 A 1-260 [» ]
1LUG X-ray 0.95 A 2-260 [» ]
1LZV X-ray 2.30 A 1-260 [» ]
1MOO X-ray 1.05 A 1-260 [» ]
1MUA X-ray 1.70 A 4-259 [» ]
1OKL X-ray 2.10 A 2-260 [» ]
1OKM X-ray 2.20 A 2-260 [» ]
1OKN X-ray 2.40 A 2-260 [» ]
1OQ5 X-ray 1.50 A 2-259 [» ]
1RAY X-ray 1.80 A 2-260 [» ]
1RAZ X-ray 1.90 A 2-260 [» ]
1RZA X-ray 1.90 A 2-260 [» ]
1RZB X-ray 1.80 A 2-260 [» ]
1RZC X-ray 1.90 A 2-260 [» ]
1RZD X-ray 1.90 A 2-260 [» ]
1RZE X-ray 1.90 A 2-260 [» ]
1T9N X-ray 2.00 A 1-259 [» ]
1TB0 X-ray 2.00 X 1-259 [» ]
1TBT X-ray 2.00 X 1-259 [» ]
1TE3 X-ray 2.00 X 1-260 [» ]
1TEQ X-ray 2.00 X 1-260 [» ]
1TEU X-ray 2.00 X 1-260 [» ]
1TG3 X-ray 1.80 A 1-260 [» ]
1TG9 X-ray 1.90 A 1-260 [» ]
1TH9 X-ray 1.63 A 1-260 [» ]
1THK X-ray 1.80 A 1-260 [» ]
1TTM X-ray 1.95 A 2-259 [» ]
1UGA X-ray 2.00 A 3-260 [» ]
1UGB X-ray 2.00 A 3-260 [» ]
1UGC X-ray 2.00 A 3-260 [» ]
1UGD X-ray 2.00 A 3-260 [» ]
1UGE X-ray 1.90 A 3-260 [» ]
1UGF X-ray 2.00 A 3-260 [» ]
1UGG X-ray 2.20 A 3-260 [» ]
1XEG X-ray 1.81 A 1-260 [» ]
1XEV X-ray 2.20 A/B/C/D 1-260 [» ]
1XPZ X-ray 2.02 A 3-260 [» ]
1XQ0 X-ray 1.76 A 2-260 [» ]
1YDA X-ray 2.10 A 2-260 [» ]
1YDB X-ray 1.90 A 2-260 [» ]
1YDC X-ray 1.95 A 2-260 [» ]
1YDD X-ray 2.10 A 2-260 [» ]
1YO0 X-ray 1.80 A 1-260 [» ]
1YO1 X-ray 1.70 A 1-260 [» ]
1YO2 X-ray 1.80 A 1-259 [» ]
1Z9Y X-ray 1.66 A 2-259 [» ]
1ZE8 X-ray 2.00 A 2-260 [» ]
1ZFK X-ray 1.56 A 2-259 [» ]
1ZFQ X-ray 1.55 A 2-259 [» ]
1ZGE X-ray 1.65 A 2-259 [» ]
1ZGF X-ray 1.75 A 2-259 [» ]
1ZH9 X-ray 1.70 A 2-259 [» ]
1ZSA X-ray 2.50 A 2-260 [» ]
1ZSB X-ray 2.00 A 2-260 [» ]
1ZSC X-ray 1.80 A 2-260 [» ]
2ABE X-ray 2.00 A 2-259 [» ]
2AW1 X-ray 1.46 A 2-260 [» ]
2AX2 X-ray 1.50 A 1-259 [» ]
2CA2 X-ray 1.90 A 2-260 [» ]
2CBA X-ray 1.54 A 2-260 [» ]
2CBB X-ray 1.67 A 2-260 [» ]
2CBC X-ray 1.88 A 2-260 [» ]
2CBD X-ray 1.67 A 2-260 [» ]
2CBE X-ray 1.82 A 2-260 [» ]
2EU2 X-ray 1.15 A 1-260 [» ]
2EU3 X-ray 1.60 A 1-260 [» ]
2EZ7 X-ray 2.00 A 1-259 [» ]
2F14 X-ray 1.71 A 2-259 [» ]
2FMG X-ray 1.60 A 1-259 [» ]
2FMZ X-ray 1.60 A 1-259 [» ]
2FNK X-ray 1.80 A 1-260 [» ]
2FNM X-ray 1.80 A 1-260 [» ]
2FNN X-ray 1.80 A 1-260 [» ]
2FOQ X-ray 1.25 A 1-259 [» ]
2FOS X-ray 1.10 A 1-259 [» ]
2FOU X-ray 0.99 A 1-259 [» ]
2FOV X-ray 1.15 A 1-259 [» ]
2GD8 X-ray 1.46 A 2-259 [» ]
2GEH X-ray 2.00 A 1-259 [» ]
2H15 X-ray 1.90 A 1-259 [» ]
2H4N X-ray 1.90 A 2-260 [» ]
2HD6 X-ray 1.80 A 2-259 [» ]
2HKK X-ray 1.90 A 1-260 [» ]
2HL4 X-ray 1.55 A 2-260 [» ]
2HNC X-ray 1.55 A 2-259 [» ]
2HOC X-ray 2.10 A 2-259 [» ]
2ILI X-ray 1.05 A 2-259 [» ]
2NNG X-ray 1.20 A 2-260 [» ]
2NNO X-ray 1.01 A 2-260 [» ]
2NNS X-ray 1.03 A 2-260 [» ]
2NNV X-ray 1.10 A 2-260 [» ]
2NWO X-ray 1.70 A 1-259 [» ]
2NWP X-ray 1.80 A 1-259 [» ]
2NWY X-ray 1.65 A 1-259 [» ]
2NWZ X-ray 1.80 A 1-259 [» ]
2NXR X-ray 1.70 A 1-259 [» ]
2NXS X-ray 1.80 A 1-259 [» ]
2NXT X-ray 1.15 A 1-260 [» ]
2O4Z X-ray 2.10 A 1-260 [» ]
2OSF X-ray 1.60 A 2-260 [» ]
2OSM X-ray 1.60 A 2-260 [» ]
2POU X-ray 1.60 A 1-259 [» ]
2POV X-ray 1.60 A 1-258 [» ]
2POW X-ray 1.75 A 1-259 [» ]
2Q1B X-ray 1.70 A 1-260 [» ]
2Q1Q X-ray 1.90 A 1-260 [» ]
2Q38 X-ray 1.95 A 1-260 [» ]
2QO8 X-ray 1.40 A 2-260 [» ]
2QOA X-ray 1.60 A 2-260 [» ]
2QP6 X-ray 1.45 A 2-260 [» ]
2VVA X-ray 1.56 X 1-260 [» ]
2VVB X-ray 1.66 X 1-260 [» ]
2WD2 X-ray 1.49 A 2-259 [» ]
2WD3 X-ray 1.80 A 2-260 [» ]
2WEG X-ray 1.10 A 2-260 [» ]
2WEH X-ray 2.09 A 2-260 [» ]
2WEJ X-ray 1.45 A 2-260 [» ]
2WEO X-ray 1.40 A 2-260 [» ]
2X7S X-ray 1.64 A 2-260 [» ]
2X7T X-ray 1.89 A 2-260 [» ]
2X7U X-ray 2.12 A 2-260 [» ]
3B4F X-ray 1.89 A 1-260 [» ]
3BET X-ray 1.85 A 2-260 [» ]
3BL0 X-ray 1.90 A 1-260 [» ]
3BL1 X-ray 2.10 A 1-260 [» ]
3C7P X-ray 1.70 A 1-260 [» ]
3CA2 X-ray 2.00 A 2-260 [» ]
3CAJ X-ray 1.80 A 1-260 [» ]
3CYU X-ray 1.70 A 1-260 [» ]
3D8W X-ray 1.70 A 1-260 [» ]
3D92 X-ray 1.10 A 1-260 [» ]
3D93 X-ray 1.10 A 1-260 [» ]
3D9Z X-ray 1.65 A 1-260 [» ]
3DAZ X-ray 1.60 A 1-260 [» ]
3DBU X-ray 1.70 A 1-260 [» ]
3DC3 X-ray 1.70 A 1-260 [» ]
3DC9 X-ray 1.60 A 1-260 [» ]
3DCC X-ray 1.60 A 1-260 [» ]
3DCS X-ray 1.80 A 1-260 [» ]
3DCW X-ray 1.50 A 1-260 [» ]
3DD0 X-ray 1.48 A 1-260 [» ]
3DD8 X-ray 1.90 A 1-260 [» ]
3DV7 X-ray 1.70 A 2-260 [» ]
3DVB X-ray 1.70 A 2-260 [» ]
3DVC X-ray 1.60 A 2-260 [» ]
3DVD X-ray 1.60 A 2-260 [» ]
3EFI X-ray 1.75 A 2-260 [» ]
3EFT X-ray 1.85 A 1-260 [» ]
3F4X X-ray 1.90 A 1-260 [» ]
3F8E X-ray 2.00 A 1-260 [» ]
3FFP X-ray 1.81 X 1-260 [» ]
3GZ0 X-ray 1.26 A 2-260 [» ]
3HFP X-ray 2.10 A 1-260 [» ]
3HKN X-ray 1.80 A 1-260 [» ]
3HKQ X-ray 1.70 A 1-260 [» ]
3HKT X-ray 2.36 A 1-260 [» ]
3HKU X-ray 1.80 A 1-260 [» ]
3HLJ X-ray 1.44 A 1-260 [» ]
3HS4 X-ray 1.10 A 1-260 [» ]
3IBI X-ray 1.93 A 2-260 [» ]
3IBL X-ray 1.55 A 2-260 [» ]
3IBN X-ray 2.20 A 2-260 [» ]
3IBU X-ray 1.41 A 2-260 [» ]
3IEO X-ray 2.00 A 1-260 [» ]
3IGP X-ray 1.65 A 1-260 [» ]
3K2F X-ray 1.98 A 1-260 [» ]
3K34 X-ray 0.90 A 1-260 [» ]
3K7K X-ray 1.90 A 1-260 [» ]
3KIG X-ray 1.39 A 1-260 [» ]
3KKX neutron diffraction 2.00 A 1-260 [» ]
3KNE X-ray 1.35 A 1-260 [» ]
3KOI X-ray 1.64 A 1-260 [» ]
3KOK X-ray 1.50 A 1-260 [» ]
3KON X-ray 1.50 A 1-260 [» ]
3KS3 X-ray 0.90 A 1-260 [» ]
3KWA X-ray 2.00 A 1-260 [» ]
3L14 X-ray 1.22 A 1-260 [» ]
3M04 X-ray 1.40 A 1-260 [» ]
3M14 X-ray 1.38 A 1-260 [» ]
3M1J X-ray 1.80 A 1-260 [» ]
3M1K X-ray 1.35 A 1-260 [» ]
3M1Q X-ray 1.69 A 1-260 [» ]
3M1W X-ray 1.38 A 1-260 [» ]
3M2N X-ray 1.65 A 1-260 [» ]
3M2X X-ray 1.87 A 1-260 [» ]
3M2Y X-ray 1.17 A 1-260 [» ]
3M2Z X-ray 1.70 A 1-260 [» ]
3M3X X-ray 1.68 A 1-260 [» ]
3M40 X-ray 1.60 A 1-260 [» ]
3M5E X-ray 1.70 A 1-260 [» ]
3M5S X-ray 1.40 A 1-260 [» ]
3M5T X-ray 1.95 A 1-260 [» ]
3M67 X-ray 1.80 A 1-260 [» ]
3M96 X-ray 1.40 A 1-260 [» ]
3M98 X-ray 1.50 A 1-260 [» ]
3MHC X-ray 1.70 A 1-260 [» ]
3MHI X-ray 1.70 A 1-260 [» ]
3MHL X-ray 1.90 A 1-260 [» ]
3MHM X-ray 1.50 A 1-260 [» ]
3MHO X-ray 1.15 A 1-260 [» ]
3ML2 X-ray 1.80 A 1-260 [» ]
3MMF X-ray 1.50 A 1-260 [» ]
3MNA X-ray 1.50 A 1-260 [» ]
3MNH X-ray 1.65 A 1-260 [» ]
3MNI X-ray 1.75 A 1-260 [» ]
3MNJ X-ray 1.75 A 1-260 [» ]
3MNK X-ray 1.75 A 1-260 [» ]
3MNU X-ray 1.80 A 2-260 [» ]
3MWO X-ray 1.40 A/B 1-260 [» ]
3MYQ X-ray 1.35 A 1-260 [» ]
3MZC X-ray 1.50 A 1-260 [» ]
3N0N X-ray 1.50 A 1-260 [» ]
3N2P X-ray 1.65 A 1-260 [» ]
3N3J X-ray 1.50 A 1-260 [» ]
3N4B X-ray 1.60 A 1-260 [» ]
3NB5 X-ray 1.80 A 1-260 [» ]
3NI5 X-ray 2.10 A 1-260 [» ]
3NJ9 X-ray 2.00 A 1-260 [» ]
3OIK X-ray 1.50 A 1-260 [» ]
3OIL X-ray 1.50 A 1-260 [» ]
3OIM X-ray 1.45 A 1-260 [» ]
3OKU X-ray 1.45 A 1-260 [» ]
3OKV X-ray 1.45 A 1-260 [» ]
3OY0 X-ray 1.60 A 1-260 [» ]
3OYQ X-ray 1.47 A 1-260 [» ]
3OYS X-ray 1.54 A 1-260 [» ]
3P3H X-ray 1.50 A 1-260 [» ]
3P3J X-ray 1.60 A 1-260 [» ]
3P44 X-ray 2.20 A 1-260 [» ]
3P4V X-ray 2.00 A 1-260 [» ]
3P55 X-ray 2.00 A 1-260 [» ]
3P58 X-ray 1.49 A 1-260 [» ]
3P5A X-ray 1.49 A 1-260 [» ]
3P5L X-ray 1.50 A 1-260 [» ]
3PJJ X-ray 1.80 A 2-260 [» ]
3PO6 X-ray 1.47 A 2-260 [» ]
3PYK X-ray 1.30 A 1-260 [» ]
3QYK X-ray 1.47 A 1-260 [» ]
3R16 X-ray 1.60 A 4-260 [» ]
3R17 X-ray 1.70 B 4-260 [» ]
3RG3 X-ray 1.90 A 1-260 [» ]
3RG4 X-ray 1.50 A 1-260 [» ]
3RGE X-ray 2.10 A 1-260 [» ]
3RJ7 X-ray 1.20 A 3-260 [» ]
3RLD X-ray 1.50 A 1-260 [» ]
3RYJ X-ray 1.39 B 2-260 [» ]
3RYV X-ray 1.20 B 2-260 [» ]
3RYX X-ray 1.60 B 2-260 [» ]
3RYY X-ray 1.16 A 2-260 [» ]
3RYZ X-ray 1.37 A 2-260 [» ]
3RZ0 X-ray 1.80 B 2-260 [» ]
3RZ1 X-ray 1.51 B 2-260 [» ]
3RZ5 X-ray 1.65 A 2-260 [» ]
3RZ7 X-ray 1.80 A 2-260 [» ]
3RZ8 X-ray 1.70 A 2-260 [» ]
3S71 X-ray 1.25 B 3-260 [» ]
3S72 X-ray 1.60 B 3-260 [» ]
3S73 X-ray 1.75 B 3-260 [» ]
3S74 X-ray 1.40 B 3-260 [» ]
3S75 X-ray 1.50 B 3-260 [» ]
3S76 X-ray 1.60 A 3-260 [» ]
3S77 X-ray 1.86 B 3-260 [» ]
3S78 X-ray 1.98 B 3-260 [» ]
3S8X X-ray 1.30 A 1-260 [» ]
3S9T X-ray 1.30 A 1-260 [» ]
3SAP X-ray 1.75 A 1-260 [» ]
3SAX X-ray 1.10 A 1-260 [» ]
3SBH X-ray 1.65 A 1-260 [» ]
3SBI X-ray 1.40 A 1-260 [» ]
3T5U X-ray 1.75 A 2-260 [» ]
3T5Z X-ray 1.65 A 2-260 [» ]
3T82 X-ray 2.00 A 1-260 [» ]
3T83 X-ray 1.80 A 1-260 [» ]
3T84 X-ray 2.00 A 1-260 [» ]
3T85 X-ray 2.40 A 1-260 [» ]
3TMJ Other 2.00 A 3-260 [» ]
3TVN X-ray 1.50 X 3-260 [» ]
3TVO X-ray 1.60 X 3-260 [» ]
3U3A X-ray 1.55 X 1-260 [» ]
3U45 X-ray 1.70 X 1-260 [» ]
3U47 X-ray 1.60 A 1-260 [» ]
3U7C X-ray 0.93 A 1-260 [» ]
3V2J X-ray 1.70 A 1-260 [» ]
3V2M X-ray 1.47 A 1-260 [» ]
3V3F X-ray 2.00 A 1-260 [» ]
3V3G X-ray 1.56 B 1-260 [» ]
3V3H X-ray 1.85 B 1-260 [» ]
3V3I X-ray 1.73 B 1-260 [» ]
3V3J X-ray 1.63 A 1-260 [» ]
3V5G X-ray 1.50 A 1-260 [» ]
3V7X X-ray 1.03 A 2-260 [» ]
3VBD X-ray 1.05 A 2-260 [» ]
3ZP9 X-ray 1.31 A 1-260 [» ]
4BCW X-ray 1.50 A 4-260 [» ]
4BF1 X-ray 1.35 A 2-260 [» ]
4BF6 X-ray 1.82 A 2-260 [» ]
4CA2 X-ray 2.10 A 1-260 [» ]
4CAC X-ray 2.20 A 2-260 [» ]
4CQ0 X-ray 1.45 A 1-260 [» ]
4DZ7 X-ray 1.49 A 1-260 [» ]
4DZ9 X-ray 1.49 A 1-260 [» ]
4E3D X-ray 1.60 A 1-260 [» ]
4E3F X-ray 1.50 A 1-260 [» ]
4E3G X-ray 1.55 A 1-260 [» ]
4E3H X-ray 1.50 A 1-260 [» ]
4E49 X-ray 1.45 A 1-260 [» ]
4E4A X-ray 1.45 A 1-260 [» ]
4E5Q X-ray 1.70 A 1-260 [» ]
4FIK X-ray 1.20 A 1-260 [» ]
4FL7 X-ray 1.85 A 2-260 [» ]
4FPT X-ray 0.98 A 1-260 [» ]
4FRC X-ray 0.98 A 1-260 [» ]
4FU5 X-ray 0.98 A 1-260 [» ]
4FVN X-ray 1.05 A 1-260 [» ]
4FVO X-ray 1.05 A 1-260 [» ]
4G0C neutron diffraction 2.00 A 4-260 [» ]
4GGE X-ray 1.47 A 1-260 [» ]
4GL1 X-ray 1.50 X 1-260 [» ]
4HBA X-ray 1.76 A 1-260 [» ]
4HEW X-ray 1.70 A 1-260 [» ]
4HEY X-ray 1.45 A 1-260 [» ]
4HEZ X-ray 1.34 A 1-260 [» ]
4HF3 X-ray 1.15 A 1-260 [» ]
4HT0 X-ray 1.60 A 1-260 [» ]
4IDR X-ray 1.60 X 3-260 [» ]
4ILX X-ray 1.60 A 4-260 [» ]
4ITO X-ray 1.16 A 1-260 [» ]
4ITP X-ray 1.70 A 4-260 [» ]
4IWZ X-ray 1.60 A 4-260 [» ]
4JS6 X-ray 1.55 A 1-260 [» ]
4JSA X-ray 1.50 A 1-260 [» ]
4JSS X-ray 1.50 A 1-260 [» ]
4JSW X-ray 1.90 A 1-260 [» ]
4JSZ X-ray 1.90 A 1-260 [» ]
4K0S X-ray 1.80 A 4-260 [» ]
4K0T X-ray 1.78 A 4-260 [» ]
4K0Z X-ray 1.80 A 3-260 [» ]
4K13 X-ray 1.60 A 4-260 [» ]
4K1Q X-ray 1.70 A 3-260 [» ]
4KAP X-ray 1.45 A 5-260 [» ]
4KNI X-ray 1.80 A 1-260 [» ]
4KNJ X-ray 2.00 A 1-260 [» ]
4L5U X-ray 2.05 A 1-260 [» ]
4L5V X-ray 1.63 A 1-260 [» ]
4L5W X-ray 1.70 A 1-260 [» ]
4LP6 X-ray 2.15 A/B 1-260 [» ]
4M2R X-ray 1.99 A 4-260 [» ]
4M2U X-ray 2.00 A 4-260 [» ]
4M2V X-ray 1.72 A 4-260 [» ]
4M2W X-ray 1.66 A 4-260 [» ]
4MDG X-ray 1.35 A 3-260 [» ]
4MDL X-ray 1.52 A 3-260 [» ]
4MDM X-ray 1.55 A 3-260 [» ]
4MO8 X-ray 1.85 A 1-260 [» ]
4MTY X-ray 1.00 A 1-260 [» ]
4N0X X-ray 1.63 B 1-260 [» ]
4N16 X-ray 1.54 A 1-260 [» ]
5CA2 X-ray 2.10 A 1-260 [» ]
5CAC X-ray 2.20 A 2-260 [» ]
6CA2 X-ray 2.50 A 1-260 [» ]
7CA2 X-ray 2.40 A 1-260 [» ]
8CA2 X-ray 2.40 A 1-260 [» ]
9CA2 X-ray 2.80 A 1-260 [» ]
ProteinModelPortali P00918.
SMRi P00918. Positions 3-260.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107215. 12 interactions.
IntActi P00918. 5 interactions.
MINTi MINT-1367766.
STRINGi 9606.ENSP00000285379.

Chemistry

BindingDBi P00918.
ChEMBLi CHEMBL2096906.
DrugBanki DB00819. Acetazolamide.
DB00436. Bendroflumethiazide.
DB00562. Benzthiazide.
DB01194. Brinzolamide.
DB00880. Chlorothiazide.
DB00606. Cyclothiazide.
DB01119. Diazoxide.
DB00869. Dorzolamide.
DB01031. Ethinamate.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB00232. Methyclothiazide.
DB01325. Quinethazone.
DB00273. Topiramate.
DB01021. Trichlormethiazide.

PTM databases

PhosphoSitei P00918.

2D gel databases

OGPi P00918.
REPRODUCTION-2DPAGE IPI00218414.
P00918.
UCD-2DPAGE P00918.

Proteomic databases

MaxQBi P00918.
PaxDbi P00918.
PeptideAtlasi P00918.
PRIDEi P00918.

Protocols and materials databases

DNASUi 760.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000285379 ; ENSP00000285379 ; ENSG00000104267 .
GeneIDi 760.
KEGGi hsa:760.
UCSCi uc003ydk.2. human.

Organism-specific databases

CTDi 760.
GeneCardsi GC08P086376.
HGNCi HGNC:1373. CA2.
HPAi CAB010102.
HPA001550.
MIMi 259730. phenotype.
611492. gene.
neXtProti NX_P00918.
Orphaneti 2785. Osteopetrosis with renal tubular acidosis.
PharmGKBi PA25989.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3338.
HOGENOMi HOG000112637.
HOVERGENi HBG002837.
InParanoidi P00918.
KOi K18245.
OMAi CFNAENE.
OrthoDBi EOG7WMCK7.
PhylomeDBi P00918.
TreeFami TF316425.

Enzyme and pathway databases

BRENDAi 4.2.1.1. 2681.
Reactomei REACT_121123. Reversible hydration of carbon dioxide.
REACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
SABIO-RK P00918.

Miscellaneous databases

ChiTaRSi CA2. human.
EvolutionaryTracei P00918.
GeneWikii Carbonic_anhydrase_II.
GenomeRNAii 760.
NextBioi 3074.
PROi P00918.
SOURCEi Search...

Gene expression databases

ArrayExpressi P00918.
Bgeei P00918.
CleanExi HS_CA2.
Genevestigatori P00918.

Family and domain databases

Gene3Di 3.10.200.10. 1 hit.
InterProi IPR018443. CA2.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF90. PTHR18952:SF90. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 1 hit.
PROSITEi PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of human liver carbonic anhydrase II cDNA."
    Montgomery J.C., Venta P.J., Tashian R.E., Hewett-Emmett D.
    Nucleic Acids Res. 15:4687-4687(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II."
    Murakami H., Marelich G.P., Grubb J.H., Kyle J.W., Sly W.S.
    Genomics 1:159-166(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Urinary bladder.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  7. "Human carbonic anhydrases. XII. The complete primary structure of the C isozyme."
    Lin K.-T.D., Deutsch H.F.
    J. Biol. Chem. 249:2329-2337(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-260, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
  8. "Primary structure of human carbonic anhydrase C."
    Henderson L.E., Henriksson D., Nyman P.O.
    J. Biol. Chem. 251:5457-5463(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-260.
  9. "Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements."
    Venta P.J., Montgomery J.C., Hewett-Emmett D., Tashian R.E.
    Biochim. Biophys. Acta 826:195-201(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
  10. "Direct extracellular interaction between carbonic anhydrase IV and the human NBC1 sodium/bicarbonate co-transporter."
    Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.
    Biochemistry 42:12321-12329(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC4A4.
  11. "Regulation of the human NBC3 Na+/HCO3- cotransporter by carbonic anhydrase II and PKA."
    Loiselle F.B., Morgan P.E., Alvarez B.V., Casey J.R.
    Am. J. Physiol. 286:C1423-C1433(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC4A7.
  12. "Molecular mechanism of kNBC1-carbonic anhydrase II interaction in proximal tubule cells."
    Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I., Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I.
    J. Physiol. (Lond.) 559:55-65(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC4A4.
  13. "Metabolon disruption: a mechanism that regulates bicarbonate transport."
    Alvarez B.V., Vilas G.L., Casey J.R.
    EMBO J. 24:2499-2511(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLC26A6, SUBCELLULAR LOCATION.
  14. "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I."
    Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T.
    Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  15. "Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide."
    Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G.
    Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Crystal structure of human carbonic anhydrase C."
    Liljas A., Kannan K.K., Bergsten P.-C., Waara I., Fridborg K., Strandberg B., Carlbom U., Jaerup L., Loevgren S., Petef M.
    Nature New Biol. 235:131-137(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  18. "Refined structure of human carbonic anhydrase II at 2.0-A resolution."
    Eriksson A.E., Jones T.A., Liljas A.
    Proteins 4:274-282(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC ION.
  19. "Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN-ion to the zinc at high pH."
    Eriksson A.E., Kylsten P.M., Jones T.A., Liljas A.
    Proteins 4:283-293(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS.
  20. "Conformational mobility of His-64 in the Thr-200TO: human carbonic anhydrase II."
    Krebs J.F., Fierke C.A., Alexander R.S., Christianson D.W.
    Biochemistry 30:9153-9160(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT SER-199 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF THR-199, BIOPHYSICOCHEMICAL PROPERTIES.
  21. "Engineering the hydrophobic pocket of carbonic anhydrase II."
    Alexander R.S., Nair S.K., Christianson D.W.
    Biochemistry 30:11064-11072(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANTS PHE-142; TYR-142 AND HIS-142 IN COMPLEX WITH INHIBITORS, MUTAGENESIS OF VAL-142.
  22. "Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121."
    Nair S.K., Calderone T.L., Christianson D.W., Fierke C.A.
    J. Biol. Chem. 266:17320-17325(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF MUTANT ALA-121, MUTAGENESIS OF VAL-121, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  23. "Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions."
    Mangani S., Haakansson K.
    Eur. J. Biochem. 210:867-871(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS, ENZYME REGULATION.
  24. "Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes."
    Haakansson K., Carlsson M., Svensson L.A., Liljas A.
    J. Mol. Biol. 227:1192-1204(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS.
  25. "Structure of cobalt carbonic anhydrase complexed with bicarbonate."
    Haakansson K., Wehnert A.
    J. Mol. Biol. 228:1212-1218(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH COBALT ION AND BICARBONATE.
  26. "Engineering the zinc binding site of human carbonic anhydrase II: structure of the His-94-->Cys apoenzyme in a new crystalline form."
    Alexander R.S., Kiefer L.L., Fierke C.A., Christianson D.W.
    Biochemistry 32:1510-1518(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT CYS-94 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF HIS-94.
  27. "Structural consequences of hydrophilic amino acid substitutions in the hydrophobic pocket of human carbonic anhydrase II."
    Nair S.K., Christianson D.W.
    Biochemistry 32:4506-4514(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT ALA-197; GLU-197; HIS-197 AND ARG-197, MUTAGENESIS OF LEU-197.
  28. "Structure of an engineered His3Cys zinc binding site in human carbonic anhydrase II."
    Ippolito J.A., Christianson D.W.
    Biochemistry 32:9901-9905(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT CYS-198 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF THR-198.
  29. "Structure and energetics of a non-proline cis-peptidyl linkage in a proline-202-->alanine carbonic anhydrase II variant."
    Tweedy N.B., Nair S.K., Paterno S.A., Fierke C.A., Christianson D.W.
    Biochemistry 32:10944-10949(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT ALA-201 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF PRO-201.
  30. "The structure of human carbonic anhydrase II in complex with bromide and azide."
    Joensson B.M., Haakansson K., Liljas A.
    FEBS Lett. 322:186-190(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS.
  31. "Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II."
    Krebs J.F., Ippolito J.A., Christianson D.W., Fierke C.A.
    J. Biol. Chem. 268:27458-27466(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT VAL-198 IN COMPLEX WITH ZINC ION AND INHIBITORS, MUTAGENESIS OF THR-198, BIOPHYSICOCHEMICAL PROPERTIES.
  32. "Crystal structure of the complex between human carbonic anhydrase II and the aromatic inhibitor 1,2,4-triazole."
    Mangani S., Liljas A.
    J. Mol. Biol. 232:9-14(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND ZINC ION.
  33. "Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-."
    Xue Y., Vidgren J., Svensson L.A., Liljas A., Jonsson B.H., Lindskog S.
    Proteins 15:80-87(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT HIS-199 IN COMPLEX WITH BICARBONATE AND ZINC ION, MUTAGENESIS OF THR-199.
  34. "Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen-bond network in human carbonic anhydrase II."
    Xue Y., Liljas A., Jonsson B.H., Lindskog S.
    Proteins 17:93-106(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANTS IN COMPLEX WITH BICARBONATE AND ZINC ION, MUTAGENESIS OF GLU-106 AND THR-198.
  35. "X-ray analysis of metal-substituted human carbonic anhydrase II derivatives."
    Haakansson K., Wehnert A., Liljas A.
    Acta Crystallogr. D 50:93-100(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH COBALT; COPPER; NICKEL AND MANGANESE IONS.
  36. "Wild-type and E106Q mutant carbonic anhydrase complexed with acetate."
    Haakansson K., Briand C., Zaitsev V., Xue Y., Liljas A.
    Acta Crystallogr. D 50:101-104(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) MUTANT GLN-106 IN COMPLEX WITH THE INHIBITOR ACETATE, MUTAGENESIS OF GLU-106.
  37. "Structural consequences of redesigning a protein-zinc binding site."
    Ippolito J.A., Christianson D.W.
    Biochemistry 33:15241-15249(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-259 OF MUTANTS ALA-94; CYS-94; CYS-96; CYS-119 AND ASP-119 IN COMPLEX WITH ZINC ION.
  38. "The structure of a complex between carbonic anhydrase II and a new inhibitor, trifluoromethane sulphonamide."
    Haakansson K., Liljas A.
    FEBS Lett. 350:319-322(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR TRIFLUOROMETHANE SULPHONAMIDE.
  39. "Positions of His-64 and a bound water in human carbonic anhydrase II upon binding three structurally related inhibitors."
    Smith G.M., Alexander R.S., Christianson D.W., McKeever B.M., Ponticello G.S., Springer J.P., Randall W.C., Baldwin J.J., Habecker C.N.
    Protein Sci. 3:118-125(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  40. "Structural basis of inhibitor affinity to variants of human carbonic anhydrase II."
    Nair S.K., Krebs J.F., Christianson D.W., Fierke C.A.
    Biochemistry 34:3981-3989(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS ARG-197; ASP-197 AND PHE-197 IN COMPLEX WITH THE INHIBITOR ACETAZOLAMIDE.
  41. "Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase II influence inhibitor binding constants."
    Boriack P.A., Christianson D.W., Kingery-Wood J., Whitesides G.M.
    J. Med. Chem. 38:2286-2291(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  42. "Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity."
    Ippolito J.A., Baird T.T. Jr., McGee S.A., Christianson D.W., Fierke C.A.
    Proc. Natl. Acad. Sci. U.S.A. 92:5017-5021(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANTS ASP-198; GLU-198 AND HIS-198 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF THR-198, BIOPHYSICOCHEMICAL PROPERTIES.
  43. "Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II."
    Huang C.C., Lesburg C.A., Kiefer L.L., Fierke C.A., Christianson D.W.
    Biochemistry 35:3439-3446(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF THE MUTANT GLN-117 IN COMPLEX WITH ZINC ION AND THE INHIBITOR ACETAZOLAMIDE, MUTAGENESIS OF GLU-117.
  44. "X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis."
    Scolnick L.R., Christianson D.W.
    Biochemistry 35:16429-16434(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS GLY-65; HIS-65; LEU-65; PHE-65; SER-65 AND THR-65 IN COMPLEX WITH ZINC ION.
  45. "Unexpected binding mode of the sulfonamide fluorophore 5-dimethylamino-1-naphthalene sulfonamide to human carbonic anhydrase II. Implications for the development of a zinc biosensor."
    Nair S.K., Elbaum D., Christianson D.W.
    J. Biol. Chem. 271:1003-1007(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR DANSYLAMIDE.
  46. "Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine."
    Briganti F., Mangani S., Orioli P., Scozzafava A., Vernaglione G., Supuran C.T.
    Biochemistry 36:10384-10392(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH THE ACTIVATOR HISTAMINE, ENZYME REGULATION.
  47. "Histidine --> carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity."
    Lesburg C.A., Huang C., Christianson D.W., Fierke C.A.
    Biochemistry 36:15780-15791(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANTS ASN-94; ASN-119 AND GLN-119 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF HIS-94 AND HIS-119, BIOPHYSICOCHEMICAL PROPERTIES.
  48. "Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: molecular basis of isozyme-drug discrimination."
    Stams T., Chen Y., Boriack-Sjodin P.A., Hurt J.D., Liao J., May J.A., Dean T., Laipis P., Silverman D.N., Christianson D.W.
    Protein Sci. 7:556-563(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR BRINZOLAMIDE.
  49. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH SULFONAMIDE INHIBITORS AND ZINC ION.
  50. "Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction?"
    Briganti F., Mangani S., Scozzafava A., Vernaglione G., Supuran C.T.
    J. Biol. Inorg. Chem. 4:528-536(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CYANAMIDE AND SUBSTRATE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  51. "Mechanism of cyanamide hydration catalyzed by carbonic anhydrase II suggested by cryogenic X-ray diffraction."
    Guerri A., Briganti F., Scozzafava A., Supuran C.T., Mangani S.
    Biochemistry 39:12391-12397(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH CYANAMIDE.
  52. "Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II."
    Cox J.D., Hunt J.A., Compher K.M., Fierke C.A., Christianson D.W.
    Biochemistry 39:13687-13694(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTANTS ILE-93/MET-95/VAL-97 AND SER-93/LEU-95/MET-97 IN COMPLEX WITH COBALT; COPPER AND ZINC IONS.
  53. "Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II."
    Duda D., Tu C., Qian M., Laipis P., Agbandje-McKenna M., Silverman D.N., McKenna R.
    Biochemistry 40:1741-1748(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX WITH 4-METHYLIMIDAZOLE, MUTAGENESIS OF HIS-64.
  54. "Fluoroaromatic-fluoroaromatic interactions between inhibitors bound in the crystal lattice of human carbonic anhydrase II."
    Kim C.Y., Chandra P.P., Jain A., Christianson D.W.
    J. Am. Chem. Soc. 123:9620-9627(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT VAL-130 IN COMPLEX WITH FLUOROAROMATIC INHIBITORS.
  55. "Crystal structure of human carbonic anhydrase II complexed with an anti-convulsant sugar sulphamate."
    Recacha R., Costanzo M.J., Maryanoff B.E., Chattopadhyay D.
    Biochem. J. 361:437-441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR SUGAR SULFAMATE RWJ-37497, ENZYME REGULATION.
  56. "Organization of an efficient carbonic anhydrase: implications for the mechanism based on structure-function studies of a T199P/C206S mutant."
    Huang S., Sjoeblom B., Sauer-Eriksson A.E., Jonsson B.H.
    Biochemistry 41:7628-7635(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF THE MUTANT PRO-198/SER-205 IN COMPLEX WITH BICARBONATE AND INHIBITORS, MUTAGENESIS OF THR-198.
  57. "Kinetic analysis of multiple proton shuttles in the active site of human carbonic anhydrase."
    Tu C., Qian M., An H., Wadhwa N.R., Duda D., Yoshioka C., Pathak Y., McKenna R., Laipis P.J., Silverman D.N.
    J. Biol. Chem. 277:38870-38876(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF THE MUTANT HIS-7, MUTAGENESIS OF TYR-7.
  58. "Structural aspects of isozyme selectivity in the binding of inhibitors to carbonic anhydrases II and IV."
    Kim C.Y., Whittington D.A., Chang J.S., Liao J., May J.A., Christianson D.W.
    J. Med. Chem. 45:888-893(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH INHIBITORS, FUNCTION.
  59. "Successful virtual screening for novel inhibitors of human carbonic anhydrase: strategy and experimental confirmation."
    Grueneberg S., Stubbs M.T., Klebe G.
    J. Med. Chem. 45:3588-3602(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  60. Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  61. "The refined atomic structure of carbonic anhydrase II at 1.05 A resolution: implications of chemical rescue of proton transfer."
    Duda D., Govindasamy L., Agbandje-McKenna M., Tu C., Silverman D.N., McKenna R.
    Acta Crystallogr. D 59:93-104(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX WITH THE INHIBITOR 4-METHYLIMIDAZOLE AND ZINC ION.
  62. "Unexpected nanomolar inhibition of carbonic anhydrase by COX-2-selective celecoxib: new pharmacological opportunities due to related binding site recognition."
    Weber A., Casini A., Heine A., Kuhn D., Supuran C.T., Scozzafava A., Klebe G.
    J. Med. Chem. 47:550-557(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
  63. "Crystal structure of human carbonic anhydrase II at 1.95 A resolution in complex with 667-coumate, a novel anti-cancer agent."
    Lloyd M.D., Pederick R.L., Natesh R., Woo L.W., Purohit A., Reed M.J., Acharya K.R., Potter B.V.
    Biochem. J. 385:715-720(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THE ANTI-CANCER AGENT 667-COUMATE.
  64. "Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II."
    Fisher Z., Hernandez Prada J.A., Tu C., Duda D., Yoshioka C., An H., Govindasamy L., Silverman D.N., McKenna R.
    Biochemistry 44:1097-1105(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), MUTAGENESIS OF ASN-62; HIS-64 AND ASN-67, BIOPHYSICOCHEMICAL PROPERTIES.
  65. "First crystal structures of human carbonic anhydrase II in complex with dual aromatase-steroid sulfatase inhibitors."
    Lloyd M.D., Thiyagarajan N., Ho Y.T., Woo L.W., Sutcliffe O.B., Purohit A., Reed M.J., Acharya K.R., Potter B.V.
    Biochemistry 44:6858-6866(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH DUAL AROMATASE-STEROID SULFATASE INHIBITORS.
  66. "Carbonic anhydrase activators: X-ray crystal structure of the adduct of human isozyme II with L-histidine as a platform for the design of stronger activators."
    Temperini C., Scozzafava A., Puccetti L., Supuran C.T.
    Bioorg. Med. Chem. Lett. 15:5136-5141(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACTIVATOR L-HISTIDINE, ENZYME REGULATION.
  67. "Carbonic anhydrase inhibitors: stacking with Phe131 determines active site binding region of inhibitors as exemplified by the X-ray crystal structure of a membrane-impermeant antitumor sulfonamide complexed with isozyme II."
    Menchise V., De Simone G., Alterio V., Di Fiore A., Pedone C., Scozzafava A., Supuran C.T.
    J. Med. Chem. 48:5721-5727(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  68. "Proton transfer in a Thr200His mutant of human carbonic anhydrase II."
    Bhatt D., Tu C., Fisher S.Z., Hernandez Prada J.A., McKenna R., Silverman D.N.
    Proteins 61:239-245(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), MUTAGENESIS OF HIS-64 AND THR-199.
  69. "Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II."
    Budayova-Spano M., Fisher S.Z., Dauvergne M.T., Agbandje-McKenna M., Silverman D.N., Myles D.A., McKenna R.
    Acta Crystallogr. F 62:6-9(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
  70. "X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes."
    Fisher S.Z., Govindasamy L., Boyle N., Agbandje-McKenna M., Silverman D.N., Blackburn G.M., McKenna R.
    Acta Crystallogr. F 62:618-622(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  71. "Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site region of the human isoform II as compared to the structurally related cyclooxygenase II 'selective' inhibitor celecoxib."
    Di Fiore A., Pedone C., D'Ambrosio K., Scozzafava A., De Simone G., Supuran C.T.
    Bioorg. Med. Chem. Lett. 16:437-442(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS VALDECOXIB AND CELECOXIB, ENZYME REGULATION.
  72. "N-hydroxyurea -- a versatile zinc binding function in the design of metalloenzyme inhibitors."
    Temperini C., Innocenti A., Scozzafava A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 16:4316-4320(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH N-HYDROXYUREA, ENZYME REGULATION.
  73. "Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of 5-amino-1,3,4-thiadiazole-2-sulfonamide and 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)-1,3,4-thiadiazole-2-sulfonamide to human isoform II."
    Menchise V., De Simone G., Di Fiore A., Scozzafava A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 16:6204-6208(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  74. "Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme."
    Temperini C., Scozzafava A., Vullo D., Supuran C.T.
    Chemistry 12:7057-7066(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH L- AND D-HISTIDINE, ENZYME REGULATION.
  75. "Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with 'two-prong' inhibitors reveal the molecular basis of high affinity."
    Jude K.M., Banerjee A.L., Haldar M.K., Manokaran S., Roy B., Mallik S., Srivastava D.K., Christianson D.W.
    J. Am. Chem. Soc. 128:3011-3018(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.99 ANGSTROMS) IN COMPLEX WITH TWO-PRONG INHIBITORS.
  76. "Carbonic anhydrase inhibitors: X-ray and molecular modeling study for the interaction of a fluorescent antitumor sulfonamide with isozyme II and IX."
    Alterio V., Vitale R.M., Monti S.M., Pedone C., Scozzafava A., Cecchi A., De Simone G., Supuran C.T.
    J. Am. Chem. Soc. 128:8329-8335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  77. "Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design."
    Temperini C., Scozzafava A., Vullo D., Supuran C.T.
    J. Med. Chem. 49:3019-3027(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH L- AND D-PHENYLALANINE, ENZYME REGULATION.
  78. "Carbonic anhydrase inhibitors: Hypoxia-activatable sulfonamides incorporating disulfide bonds that target the tumor-associated isoform IX."
    De Simone G., Vitale R.M., Di Fiore A., Pedone C., Scozzafava A., Montero J.-L., Winum J.-Y., Supuran C.T.
    J. Med. Chem. 49:5544-5551(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  79. "Carbonic anhydrase inhibitors: clash with Ala65 as a means for designing inhibitors with low affinity for the ubiquitous isozyme II, exemplified by the crystal structure of the topiramate sulfamide analogue."
    Winum J.Y., Temperini C., El Cheikh K., Innocenti A., Vullo D., Ciattini S., Montero J.-L., Scozzafava A., Supuran C.T.
    J. Med. Chem. 49:7024-7031(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  80. "2-substituted estradiol bis-sulfamates, multitargeted antitumor agents: synthesis, in vitro SAR, protein crystallography, and in vivo activity."
    Leese M.P., Leblond B., Smith A., Newman S.P., Di Fiore A., De Simone G., Supuran C.T., Purohit A., Reed M.J., Potter B.V.
    J. Med. Chem. 49:7683-7696(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  81. "Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste."
    Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G.
    Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SACCHARIN, ENZYME REGULATION.
  82. "Atomic crystal and molecular dynamics simulation structures of human carbonic anhydrase II: insights into the proton transfer mechanism."
    Fisher S.Z., Maupin C.M., Budayova-Spano M., Govindasamy L., Tu C., Agbandje-McKenna M., Silverman D.N., Voth G.A., McKenna R.
    Biochemistry 46:2930-2937(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
  83. "Speeding up proton transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitutions in the active site of human carbonic anhydrase II."
    Fisher S.Z., Tu C., Bhatt D., Govindasamy L., Agbandje-McKenna M., McKenna R., Silverman D.N.
    Biochemistry 46:3803-3813(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), MUTAGENESIS OF TYR-7; ASN-62 AND ASN-67, BIOPHYSICOCHEMICAL PROPERTIES.
  84. "Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV."
    Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 17:628-635(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ACTIVATOR L-ADRENALINE, ENZYME REGULATION.
  85. "Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties."
    Di Fiore A., Scozzafava A., Winum J.-Y., Montero J.-L., Pedone C., Supuran C.T., De Simone G.
    Bioorg. Med. Chem. Lett. 17:1726-1731(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  86. "Carbonic anhydrase inhibitors: the X-ray crystal structure of the adduct of N-hydroxysulfamide with isozyme II explains why this new zinc binding function is effective in the design of potent inhibitors."
    Temperini C., Winum J.Y., Montero J.L., Scozzafava A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 17:2795-2801(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR N-HYDROXYSULFAMIDE.
  87. "Carbonic anhydrase inhibitors: inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides -- solution and crystallographic studies."
    Alterio V., De Simone G., Monti S.M., Scozzafava A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 17:4201-4207(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
  88. "Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and X-ray crystallographic studies."
    Temperini C., Innocenti A., Mastrolorenzo A., Scozzafava A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 17:4866-4872(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
  89. "Location of binding sites in small molecule rescue of human carbonic anhydrase II."
    Bhatt D., Fisher S.Z., Tu C., McKenna R., Silverman D.N.
    Biophys. J. 92:562-570(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH 4-METHYLIMIDAZOLE, MUTAGENESIS OF TRP-5 AND HIS-64.
  90. "Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II."
    Srivastava D.K., Jude K.M., Banerjee A.L., Haldar M., Manokaran S., Kooren J., Mallik S., Christianson D.W.
    J. Am. Chem. Soc. 129:5528-5537(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.01 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  91. Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITOR THIOXOLONE, ENZYME REGULATION.
  92. "Role of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II."
    Zheng J., Avvaru B.S., Tu C., McKenna R., Silverman D.N.
    Biochemistry 47:12028-12036(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF MUTANTS, MUTAGENESIS OF ASN-62, BIOPHYSICOCHEMICAL PROPERTIES.
  93. "Carbonic anhydrase inhibitors. Interaction of 2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide with 12 mammalian isoforms: kinetic and X-ray crystallographic studies."
    Guezel O., Temperini C., Innocenti A., Scozzafava A., Salman A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 18:152-158(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
  94. "Carbonic anhydrase inhibitors. Interaction of 2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide with 12 mammalian isoforms: kinetic and X-ray crystallographic studies."
    Temperini C., Cecchi A., Boyle N.A., Scozzafava A., Cabeza J.E., Wentworth P. Jr., Blackburn G.M., Supuran C.T.
    Bioorg. Med. Chem. Lett. 18:999-1005(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
  95. "Carbonic anhydrase inhibitors. Interaction of indapamide and related diuretics with 12 mammalian isozymes and X-ray crystallographic studies for the indapamide-isozyme II adduct."
    Temperini C., Cecchi A., Scozzafava A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 18:2567-2573(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
  96. "Carbonic anhydrase inhibitors: the X-ray crystal structure of ethoxzolamide complexed to human isoform II reveals the importance of thr200 and gln92 for obtaining tight-binding inhibitors."
    Di Fiore A., Pedone C., Antel J., Waldeck H., Witte A., Wurl M., Scozzafava A., Supuran C.T., De Simone G.
    Bioorg. Med. Chem. Lett. 18:2669-2674(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  97. "Carbonic anhydrase inhibitors. Interaction of the antitumor sulfamate EMD 486019 with twelve mammalian carbonic anhydrase isoforms: Kinetic and X-ray crystallographic studies."
    Temperini C., Innocenti A., Scozzafava A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 18:4282-4286(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
  98. "Carbonic anhydrase inhibitors: binding of indanesulfonamides to the human isoform II."
    D'Ambrosio K., Masereel B., Thiry A., Scozzafava A., Supuran C.T., De Simone G.
    ChemMedChem 3:473-477(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH INHIBITORS INDANESULFONAMIDES.
  99. "Structure of a (129)Xe-cryptophane biosensor complexed with human carbonic anhydrase II."
    Aaron J.A., Chambers J.M., Jude K.M., Di Costanzo L., Dmochowski I.J., Christianson D.W.
    J. Am. Chem. Soc. 130:6942-6943(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH (129)XE-CRYPTOPHANE BIOSENSOR.
  100. "Entrapment of carbon dioxide in the active site of carbonic anhydrase II."
    Domsic J.F., Avvaru B.S., Kim C.U., Gruner S.M., Agbandje-McKenna M., Silverman D.N., McKenna R.
    J. Biol. Chem. 283:30766-30771(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH CO2.
  101. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  102. "Carbonic anhydrase inhibitors: bioreductive nitro-containing sulfonamides with selectivity for targeting the tumor associated isoforms IX and XII."
    D'Ambrosio K., Vitale R.-M., Dogne J.-M., Masereel B., Innocenti A., Scozzafava A., De Simone G., Supuran C.T.
    J. Med. Chem. 51:3230-3237(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
  103. "Anticancer steroid sulfatase inhibitors: synthesis of a potent fluorinated second-generation agent, in vitro and in vivo activities, molecular modeling, and protein crystallography."
    Woo L.W.L., Fischer D.S., Sharland C.M., Trusselle M., Foster P.A., Chander S.K., Di Fiore A., Supuran C.T., De Simone G., Purohit A., Reed M.J., Potter B.V.L.
    Mol. Cancer Ther. 7:2435-2444(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  104. "Design of a carbonic anhydrase IX active-site mimic to screen inhibitors for possible anticancer properties."
    Genis C., Sippel K.H., Case N., Cao W., Avvaru B.S., Tartaglia L.J., Govindasamy L., Tu C., Agbandje-McKenna M., Silverman D.N., Rosser C.J., McKenna R.
    Biochemistry 48:1322-1331(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION, MUTAGENESIS OF ALA-65 AND ASN-67.
  105. "Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network."
    Avvaru B.S., Busby S.A., Chalmers M.J., Griffin P.R., Venkatakrishnan B., Agbandje-McKenna M., Silverman D.N., McKenna R.
    Biochemistry 48:7365-7372(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) FREE AND IN COMPLEX WITH ZINC ION, COFACTOR.
  106. "A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases."
    Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITOR THIABENDAZOLE-5-SULFONAMIDE, ENZYME REGULATION.
  107. "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors."
    Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T.
    J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-260 IN COMPLEX WITH COUMARIN INHIBITORS, ENZYME REGULATION.
  108. "Carbonic anhydrase inhibitors. Comparison of chlorthalidone and indapamide X-ray crystal structures in adducts with isozyme II: when three water molecules and the keto-enol tautomerism make the difference."
    Temperini C., Cecchi A., Scozzafava A., Supuran C.T.
    J. Med. Chem. 52:322-328(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  109. "Carbonic anhydrase inhibitors. Comparison of aliphatic sulfamate/bis-sulfamate adducts with isozymes II and IX as a platform for designing tight-binding, more isoform-selective inhibitors."
    Vitale R.M., Alterio V., Innocenti A., Winum J.-Y., Monti S.M., De Simone G., Supuran C.T.
    J. Med. Chem. 52:5990-5998(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  110. "S-glycosyl primary sulfonamides--a new structural class for selective inhibition of cancer-associated carbonic anhydrases."
    Lopez M., Paul B., Hofmann A., Morizzi J., Wu Q.K., Charman S.A., Innocenti A., Vullo D., Supuran C.T., Poulsen S.-A.
    J. Med. Chem. 52:6421-6432(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITORS.
  111. "Dissecting the inhibition mechanism of cytosolic versus transmembrane carbonic anhydrases by ESR."
    Ciani L., Cecchi A., Temperini C., Supuran C.T., Ristori S.
    J. Phys. Chem. B 113:13998-14005(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
  112. "Structural study of X-ray induced activation of carbonic anhydrase."
    Sjoeblom B., Polentarutti M., Djinovic-Carugo K.
    Proc. Natl. Acad. Sci. U.S.A. 106:10609-10613(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, ENZYME REGULATION.
  113. "Chemical and enzymological characterization of an Indonesian variant of human erythrocyte carbonic anhydrase II, CAII Jogjakarta (17 Lys leads to Glu)."
    Jones G.L., Sofro A.S.M., Shaw D.C.
    Biochem. Genet. 20:979-1000(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT JOGJAKARTA GLU-18.
  114. "A chemical and enzymological comparison of the common major human erythrocyte carbonic anhydrase II, its minor component, and a new genetic variant, CA II Melbourne (237 Pro leads to His)."
    Jones G.L., Shaw D.C.
    Hum. Genet. 63:392-399(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MELBOURNE HIS-236.
  115. "Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His-->Tyr): complete structure of the normal human CA II gene."
    Venta P.J., Welty R.J., Johnson T.M., Sly W.S., Tashian R.E.
    Am. J. Hum. Genet. 49:1082-1090(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OPTB3 TYR-107.
  116. "Molecular basis of human carbonic anhydrase II deficiency."
    Roth D.E., Venta P.J., Tashian R.E., Sly W.S.
    Proc. Natl. Acad. Sci. U.S.A. 89:1804-1808(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OPTB3 TYR-107.
  117. "A point mutation in exon 3 (His 107-->Tyr) in two unrelated Japanese patients with carbonic anhydrase II deficiency with central nervous system involvement."
    Soda H., Yukizane S., Yoshida I., Koga Y., Aramaki S., Kato H.
    Hum. Genet. 97:435-437(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OPTB3 TYR-107.
  118. "Seven novel mutations in carbonic anhydrase II deficiency syndrome identified by SSCP and direct sequencing analysis."
    Hu P.Y., Lim E.J., Ciccolella J., Strisciuglio P., Sly W.S.
    Hum. Mutat. 9:383-387(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OPTB3 PRO-92.
  119. "Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal tubular acidosis and brain calcification): novel mutations in CA2 identified by direct sequencing expand the opportunity for genotype-phenotype correlation."
    Shah G.N., Bonapace G., Hu P.Y., Strisciuglio P., Sly W.S.
    Hum. Mutat. 24:272-272(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS OPTB3 PRO-92; TYR-94; TYR-107 AND ARG-144, CHARACTERIZATION OF VARIANTS TYR-94 AND ARG-144.

Entry informationi

Entry nameiCAH2_HUMAN
AccessioniPrimary (citable) accession number: P00918
Secondary accession number(s): B2R7G8, Q6FI12, Q96ET9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 187 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Target of drugs used in treatments against glaucoma disorder and breast cancer.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi