P00918 (CAH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

CA2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	260 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for bone resorption and osteoclast differentiation By similarity. Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Ref.49 Ref.57
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Zinc. Can also use cobalt(II) with lower efficiency, but not copper(II), nickel(II) and manganese(II). Ref.104
Enzyme regulation	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. Ref.13 Ref.14 Ref.21 Ref.22 Ref.45 Ref.54 Ref.61 Ref.65 Ref.70 Ref.71 Ref.73 Ref.76 Ref.80 Ref.83 Ref.86 Ref.87 Ref.90 Ref.92 Ref.93 Ref.94 Ref.96 Ref.101 Ref.103 Ref.105 Ref.106 Ref.110 Ref.111
Subunit structure	Interacts with SLC4A4. Interaction with SLC4A7 regulates SLC4A7 transporter activity. Ref.10 Ref.11 Ref.12
Subcellular location	Cytoplasm.
Involvement in disease	Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:259730]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder 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. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation. Ref.114 Ref.115 Ref.116 Ref.117 Ref.118
Miscellaneous	Target of drugs used in treaments against glaucoma disorder and breast cancer.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.
Biophysicochemical properties	Absorption: Abs(max)=550 nm Ref.14 Ref.19 Ref.21 Ref.30 Ref.41 Ref.46 Ref.49 Ref.63 Ref.82 Ref.91 At pH 7.0. Shows a second maximum at 618 nm. Kinetic parameters: KM=10 mM for CO2 KM=82 mM for H2CO3 KM=3 mM for 4-nitrophenyl acetate pH dependence: Optimum pH is 6-8.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Disease	Disease mutation Osteopetrosis
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	apical part of cell Inferred from direct assay. Source: UniProtKB
Molecular function	carbonate dehydratase activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from direct assay Ref.18. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7 Ref.8

Chain

2 – 260

259

Carbonic anhydrase 2

PRO_0000077418

Regions

Region

198 – 199

2

Substrate binding

Sites

Active site

64

1

Active site

67

1

Active site

127

1

Metal binding

94

1

Zinc; catalytic Ref.16

Metal binding

96

1

Zinc; catalytic

Metal binding

119

1

Zinc; catalytic

Binding site

62

1

Activator

Binding site

67

1

Activator

Binding site

92

1

Activator

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.8

Natural variations

Natural variant

18

1

K → E in Jogjakarta. Ref.112

VAR_001380

Natural variant

92

1

Q → P in OPTB3; in Czechoslovakia. Ref.117 Ref.118

VAR_001381

Natural variant

94

1

H → Y in OPTB3; partial loss of activity. Ref.118

VAR_021009

Natural variant

107

1

H → Y in OPTB3; frequent mutation. Ref.114 Ref.115 Ref.116 Ref.118

VAR_001382

Natural variant

144

1

G → R in OPTB3; complete loss of activity. Ref.118

VAR_021010

Natural variant

236

1

P → H in Melbourne. Ref.113

VAR_001383

Natural variant

252

1

N → D.
Corresponds to variant rs2228063 [ dbSNP | Ensembl ].

VAR_001384

Experimental info

Mutagenesis

5

1

W → A: Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with W-64. Ref.88

Mutagenesis

7

1

Y → F: Enhanced activity. Ref.56 Ref.82

Mutagenesis

7

1

Y → H: Reduced proton transfer rate. Ref.56 Ref.82

Mutagenesis

62

1

N → A: Reduced activity. Ref.63 Ref.82 Ref.91

Mutagenesis

62

1

N → D: Strongly reduced activity. Ref.63 Ref.82 Ref.91

Mutagenesis

62

1

N → H: Reduced proton transfer; when associated with A-64. Ref.63 Ref.82 Ref.91

Mutagenesis

62

1

N → L: Reduced activity. Ref.63 Ref.82 Ref.91

Mutagenesis

62

1

N → T: Reduced activity. Ref.63 Ref.82 Ref.91

Mutagenesis

62

1

N → V: Reduced activity. Ref.63 Ref.82 Ref.91

Mutagenesis

64

1

H → 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. Ref.52 Ref.63 Ref.67 Ref.88

Mutagenesis

64

1

H → G: Impaired activity, not rescued by 4-methylimidazole (4-MI). Ref.52 Ref.63 Ref.67 Ref.88

Mutagenesis

64

1

H → W: Impaired activity, rescued by 4-methylimidazole (4-MI). Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with A-5. Ref.52 Ref.63 Ref.67 Ref.88

Mutagenesis

65

1

A → F: Reduced activity. Ref.103

Mutagenesis

65

1

A → H, L or S: Normal activity. Ref.103

Mutagenesis

67

1

N → H: Enhanced proton transfer; when associated with A-64. Ref.63 Ref.82 Ref.103

Mutagenesis

67

1

N → L: Reduced activity. Ref.63 Ref.82 Ref.103

Mutagenesis

67

1

N → Q: Normal activity. Ref.63 Ref.82 Ref.103

Mutagenesis

94

1

H → C, D, E, N or Q: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities, impaired stability of zinc binding. Ref.25 Ref.46

Mutagenesis

106

1

E → A or Q: Strongly reduced CO(2) hydrase activity. Ref.33 Ref.35

Mutagenesis

106

1

E → D: Normal CO(2) hydrase activity. Ref.33 Ref.35

Mutagenesis

117

1

E → Q: Strongly reduced activity and sulfonamide affinity. Ref.42

Mutagenesis

119

1

H → D, N or Q: Reduced activity. Ref.46

Mutagenesis

119

1

H → E: Strongly reduced activity. Ref.46

Mutagenesis

121

1

V → A, G, I, L or S: Reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. Ref.21

Mutagenesis

121

1

V → K or R: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. Ref.21

Mutagenesis

142

1

V → F or Y: Strongly impaired activity. Ref.20

Mutagenesis

142

1

V → G: Weakly impaired activity. Ref.20

Mutagenesis

142

1

V → H: Impaired activity. Ref.20

Mutagenesis

197

1

L → A: Reduced CO(2) hydrase activity. Ref.26

Mutagenesis

197

1

L → E, H or R: Strongly reduced CO(2) hydrase activity. Ref.26

Mutagenesis

197

1

L → F: Normal activity. Ref.26

Mutagenesis

198

1

T → A, C, H or P: Strongly reduced activity. Ref.27 Ref.30 Ref.33 Ref.41 Ref.55

Mutagenesis

198

1

T → D or E: Strongly reduced activity, but enhanced zinc affinity. Ref.27 Ref.30 Ref.33 Ref.41 Ref.55

Mutagenesis

198

1

T → S or V: Reduced activity. Ref.27 Ref.30 Ref.33 Ref.41 Ref.55

Mutagenesis

199

1

T → H: Higher affinity for bicarbonate. Enhanced proton transfer capacity; when associated with A-64. Ref.19 Ref.32 Ref.67

Mutagenesis

199

1

T → S: Enhanced p-nitrophenyl acetate esterase activity, but normal CO(2) hydrase activity. Ref.19 Ref.32 Ref.67

Mutagenesis

201

1

P → A: Normal CO(2) hydrase activity, but impaired stability. Ref.28

Sequence conflict

179 – 180

2

DP → AA in AAH11949. Ref.6

Secondary structure

1

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260

Helix Strand Turn

Details...

Turn

9 – 11

3

Turn

13 – 15

3

Helix

16 – 18

3

Helix

21 – 24

4

Beta strand

25 – 27

3

Turn

35 – 37

3

Beta strand

45 – 50

6

Beta strand

56 – 61

6

Beta strand

63 – 70

8

Beta strand

73 – 75

3

Beta strand

77 – 82

6

Beta strand

88 – 97

10

Beta strand

106 – 109

4

Beta strand

115 – 124

10

Helix

125 – 127

3

Helix

130 – 133

4

Beta strand

139 – 151

13

Helix

154 – 156

3

Helix

157 – 162

6

Helix

163 – 165

3

Beta strand

172 – 174

3

Helix

180 – 183

4

Beta strand

190 – 195

6

Beta strand

206 – 213

8

Beta strand

215 – 217

3

Helix

219 – 225

7

Beta strand

229 – 231

3

Beta strand

256 – 258

3

Sequences

	Sequence		Length	Mass (Da)
	P00918 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 2EC2BB7548F10558	FASTA	260	29,246
	10 20 30 40 50 60 MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS YDQATSLRIL 70 80 90 100 110 120 NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL DGQGSEHTVD KKKYAAELHL 130 140 150 160 170 180 VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG SAKPGLQKVV DVLDSIKTKG KSADFTNFDP 190 200 210 220 230 240 RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM 250 260 VDNWRPAQPL KNRQIKASFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3108857] [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: 3121496] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Urinary bladder.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 4207120] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-260.
[8]	"Primary structure of human carbonic anhydrase C." Henderson L.E., Henriksson D., Nyman P.O. J. Biol. Chem. 251:5457-5463(1976) [PubMed: 823150] [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: 3000449] [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: 14567693] [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: 14736710] [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: 15218065] [Abstract] Cited for: INTERACTION WITH SLC4A4.
[13]	"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: 17314045] [Abstract] Cited for: ENZYME REGULATION.
[14]	"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: 18618712] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"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: 4621826] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[17]	"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: 3151019] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC ION.
[18]	"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: 3151020] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS.
[19]	"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: 1909891] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT SER-199 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF THR-199, BIOPHYSICOCHEMICAL PROPERTIES.
[20]	"Engineering the hydrophobic pocket of carbonic anhydrase II." Alexander R.S., Nair S.K., Christianson D.W. Biochemistry 30:11064-11072(1991) [PubMed: 1932029] [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.
[21]	"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: 1910042] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF MUTANT ALA-121, MUTAGENESIS OF VAL-121, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[22]	"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: 1336460] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS, ENZYME REGULATION.
[23]	"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: 1433293] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS.
[24]	"Structure of cobalt carbonic anhydrase complexed with bicarbonate." Haakansson K., Wehnert A. J. Mol. Biol. 228:1212-1218(1992) [PubMed: 1474587] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH COBALT ION AND BICARBONATE.
[25]	"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: 8431430] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT CYS-94 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF HIS-94.
[26]	"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: 8485129] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT ALA-197; GLU-197; HIS-197 AND ARG-197, MUTAGENESIS OF LEU-197.
[27]	"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: 8399159] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT CYS-198 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF THR-198.
[28]	"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: 8218160] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT ALA-201 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF PRO-201.
[29]	"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: 8482389] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS.
[30]	"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: 8262987] [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.
[31]	"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: 8331673] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND ZINC ION.
[32]	"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: 8451242] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT HIS-199 IN COMPLEX WITH BICARBONATE AND ZINC ION, MUTAGENESIS OF THR-199.
[33]	"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: 7901850] [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.
[34]	"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: 15299481] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH COBALT; COPPER; NICKEL AND MANGANESE IONS.
[35]	"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: 15299482] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) MUTANT GLN-106 IN COMPLEX WITH THE INHIBITOR ACETATE, MUTAGENESIS OF GLU-106.
[36]	"Structural consequences of redesigning a protein-zinc binding site." Ippolito J.A., Christianson D.W. Biochemistry 33:15241-15249(1994) [PubMed: 7803386] [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.
[37]	"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: 8070585] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR TRIFLUOROMETHANE SULPHONAMIDE.
[38]	"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: 8142888] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[39]	"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: 7696263] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS ARG-197; ASP-197 AND PHE-197 IN COMPLEX WITH THE INHIBITOR ACETAZOLAMIDE.
[40]	"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: 7608893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[41]	"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: 7761440] [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.
[42]	"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: 8639494] [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.
[43]	"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: 8987974] [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.
[44]	"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: 8557623] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR DANSYLAMIDE.
[45]	"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: 9265618] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH THE ACTIVATOR HISTAMINE, ENZYME REGULATION.
[46]	"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: 9398308] [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.
[47]	"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: 9541386] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR BRINZOLAMIDE.
[48]	"Structural analysis of inhibitor binding to human carbonic anhydrase II." Boriack-Sjodin P.A., Zeitlin S., Chen H.H., Crenshaw L., Gross S., Dantanarayana A., Delgado P., May J.A., Dean T., Christianson D.W. Protein Sci. 7:2483-2489(1998) [PubMed: 9865942] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH SULFONAMIDE INHIBITORS AND ZINC ION.
[49]	"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: 10550681] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CYANAMIDE AND SUBSTRATE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[50]	"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: 11015219] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH CYANAMIDE.
[51]	"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: 11076507] [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.
[52]	"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: 11327835] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX WITH 4-METHYLIMIDAZOLE, MUTAGENESIS OF HIS-64.
[53]	"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: 11572683] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT VAL-130 IN COMPLEX WITH FLUOROAROMATIC INHIBITORS.
[54]	"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: 11802772] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR SUGAR SULFAMATE RWJ-37497, ENZYME REGULATION.
[55]	"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: 12056894] [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.
[56]	"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: 12171926] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF THE MUTANT HIS-7, MUTAGENESIS OF TYR-7.
[57]	"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: 11831900] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH INHIBITORS, FUNCTION.
[58]	"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: 12166932] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[59]	"Combinatorial computational method gives new picomolar ligands for a known enzyme." Grzybowski B.A., Ishchenko A.V., Kim C.Y., Topalov G., Chapman R., Christianson D.W., Whitesides G.M., Shakhnovich E.I. Proc. Natl. Acad. Sci. U.S.A. 99:1270-1273(2002) [PubMed: 11818565] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[60]	"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: 12499545] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX WITH THE INHIBITOR 4-METHYLIMIDAZOLE AND ZINC ION.
[61]	"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: 14736236] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[62]	"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: 15453828] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THE ANTI-CANCER AGENT 667-COUMATE.
[63]	"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: 15667203] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), MUTAGENESIS OF ASN-62; HIS-64 AND ASN-67, BIOPHYSICOCHEMICAL PROPERTIES.
[64]	"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: 15865431] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH DUAL AROMATASE-STEROID SULFATASE INHIBITORS.
[65]	"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: 16214338] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACTIVATOR L-HISTIDINE, ENZYME REGULATION.
[66]	"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: 16134940] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[67]	"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: 16106378] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), MUTAGENESIS OF HIS-64 AND THR-199.
[68]	"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: 16511248] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
[69]	"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: 16820676] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[70]	"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: 16290146] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS VALDECOXIB AND CELECOXIB, ENZYME REGULATION.
[71]	"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: 16759856] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH N-HYDROXYUREA, ENZYME REGULATION.
[72]	"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: 17000110] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[73]	"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: 16807956] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH L- AND D-HISTIDINE, ENZYME REGULATION.
[74]	"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: 16506782] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.99 ANGSTROMS) IN COMPLEX WITH TWO-PRONG INHIBITORS.
[75]	"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: 16787097] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[76]	"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: 16686544] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH L- AND D-PHENYLALANINE, ENZYME REGULATION.
[77]	"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: 16942027] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[78]	"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: 17125255] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[79]	"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: 17181151] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[80]	"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: 17705204] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SACCHARIN, ENZYME REGULATION.
[81]	"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: 17319692] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
[82]	"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: 17330962] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), MUTAGENESIS OF TYR-7; ASN-62 AND ASN-67, BIOPHYSICOCHEMICAL PROPERTIES.
[83]	"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: 17127057] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ACTIVATOR L-ADRENALINE, ENZYME REGULATION.
[84]	"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: 17251017] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[85]	"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: 17346964] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR N-HYDROXYSULFAMIDE.
[86]	"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: 17540563] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[87]	"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: 17588751] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[88]	"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: 17071654] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH 4-METHYLIMIDAZOLE, MUTAGENESIS OF TRP-5 AND HIS-64.
[89]	"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: 17407288] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.01 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[90]	"Inhibition of carbonic anhydrase II by thioxolone: a mechanistic and structural study." Barrese A.A. III, Genis C., Fisher S.Z., Orwenyo J.N., Kumara M.T., Dutta S.K., Phillips E., Kiddle J.J., Tu C., Silverman D.N., Govindasamy L., Agbandje-McKenna M., McKenna R., Tripp B.C. Biochemistry 47:3174-3184(2008) [PubMed: 18266323] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITOR THIOXOLONE, ENZYME REGULATION.
[91]	"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: 18942852] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF MUTANTS, MUTAGENESIS OF ASN-62, BIOPHYSICOCHEMICAL PROPERTIES.
[92]	"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: 18024029] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[93]	"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: 18162396] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[94]	"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: 18374572] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[95]	"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: 18359629] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[96]	"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: 18640037] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[97]	"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: 18161740] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH INHIBITORS INDANESULFONAMIDES.
[98]	"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: 18461940] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH (129)XE-CRYPTOPHANE BIOSENSOR.
[99]	"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: 18768466] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH CO2.
[100]	"Structure-activity relationships of C-17 cyano-substituted estratrienes as anticancer agents." Leese M.P., Jourdan F.L., Gaukroger K., Mahon M.F., Newman S.P., Foster P.A., Stengel C., Regis-Lydi S., Ferrandis E., Di Fiore A., De Simone G., Supuran C.T., Purohit A., Reed M.J., Potter B.V. J. Med. Chem. 51:1295-1308(2008) [PubMed: 18260615] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[101]	"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: 18481843] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[102]	"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: 18723489] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[103]	"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: 19170619] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION, MUTAGENESIS OF ALA-65 AND ASN-67.
[104]	"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: 19583303] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) FREE AND IN COMPLEX WITH ZINC ION, COFACTOR.
[105]	"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: 19186056] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITOR THIABENDAZOLE-5-SULFONAMIDE, ENZYME REGULATION.
[106]	"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: 19206230] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-260 IN COMPLEX WITH COUMARIN INHIBITORS, ENZYME REGULATION.
[107]	"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: 19115843] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[108]	"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: 19731956] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[109]	"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: 19827837] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITORS.
[110]	"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: 19778001] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[111]	"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: 19520834] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, ENZYME REGULATION.
[112]	"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: 6817747] [Abstract] Cited for: VARIANT JOGJAKARTA GLU-18.
[113]	"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: 6407977] [Abstract] Cited for: VARIANT MELBOURNE HIS-236.
[114]	"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: 1928091] [Abstract] Cited for: VARIANT OPTB3 TYR-107.
[115]	"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: 1542674] [Abstract] Cited for: VARIANT OPTB3 TYR-107.
[116]	"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: 8834238] [Abstract] Cited for: VARIANT OPTB3 TYR-107.
[117]	"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: 9143915] [Abstract] Cited for: VARIANT OPTB3 PRO-92.
[118]	"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: 15300855] [Abstract] Cited for: VARIANTS OPTB3 PRO-92; TYR-94; TYR-107 AND ARG-144, CHARACTERIZATION OF VARIANTS TYR-94 AND ARG-144.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00218414.

PIR

CRHU2. A27175.

RefSeq

NP_000058.1. NM_000067.2.

UniGene

Hs.155097.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
12CA	X-ray	2.40	A	2-260	[»]
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	2-260	[»]
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	2-260	[»]
1CNX	X-ray	1.90	A	2-260	[»]
1CNY	X-ray	2.30	A	2-260	[»]
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	2-258	[»]
1CVE	X-ray	2.25	A	2-260	[»]
1CVF	X-ray	2.25	A	2-260	[»]
1CVH	X-ray	2.30	A	2-259	[»]
1DCA	X-ray	2.20	A	2-260	[»]
1DCB	X-ray	2.10	A	2-260	[»]
1EOU	X-ray	2.10	A	2-260	[»]
1F2W	X-ray	1.90	A	2-260	[»]
1FQL	X-ray	2.00	A	2-260	[»]
1FQM	X-ray	2.00	A	2-260	[»]
1FQN	X-ray	2.00	A	2-260	[»]
1FQR	X-ray	2.00	A	2-260	[»]
1FR4	X-ray	1.60	A	2-260	[»]
1FR7	X-ray	1.50	A/B	2-260	[»]
1FSN	X-ray	2.00	A/B	2-260	[»]
1FSQ	X-ray	2.00	A/B	2-260	[»]
1FSR	X-ray	2.00	A/B	2-260	[»]
1G0E	X-ray	1.60	A	2-260	[»]
1G0F	X-ray	1.60	A	2-260	[»]
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	2-259	[»]
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	2-260	[»]
1HEA	X-ray	2.00	A	2-260	[»]
1HEB	X-ray	2.00	A	2-260	[»]
1HEC	X-ray	2.00	A	2-260	[»]
1HED	X-ray	2.00	A	2-260	[»]
1HVA	X-ray	2.30	A	2-260	[»]
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	2-260	[»]
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	2-260	[»]
1KWR	X-ray	2.25	A	2-260	[»]
1LG5	X-ray	1.75	A	2-260	[»]
1LG6	X-ray	2.20	A	2-260	[»]
1LGD	X-ray	1.90	A	2-260	[»]
1LUG	X-ray	0.95	A	2-260	[»]
1LZV	X-ray	2.30	A	2-260	[»]
1MOO	X-ray	1.05	A	2-260	[»]
1MUA	X-ray	1.70	A	2-260	[»]
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	2-260	[»]
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	2-260	[»]
1TB0	X-ray	2.00	X	2-260	[»]
1TBT	X-ray	2.00	X	2-260	[»]
1TE3	X-ray	2.00	X	2-260	[»]
1TEQ	X-ray	2.00	X	2-260	[»]
1TEU	X-ray	2.00	X	2-260	[»]
1TG3	X-ray	1.80	A	2-260	[»]
1TG9	X-ray	1.90	A	2-260	[»]
1TH9	X-ray	1.63	A	2-260	[»]
1THK	X-ray	1.80	A	2-260	[»]
1TTM	X-ray	1.95	A	2-260	[»]
1UGA	X-ray	2.00	A	2-260	[»]
1UGB	X-ray	2.00	A	2-260	[»]
1UGC	X-ray	2.00	A	2-260	[»]
1UGD	X-ray	2.00	A	2-260	[»]
1UGE	X-ray	1.90	A	2-260	[»]
1UGF	X-ray	2.00	A	2-260	[»]
1UGG	X-ray	2.20	A	2-260	[»]
1XEG	X-ray	1.81	A	2-260	[»]
1XEV	X-ray	2.20	A/B/C/D	2-260	[»]
1XPZ	X-ray	2.02	A	2-260	[»]
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	2-260	[»]
1YO1	X-ray	1.70	A	2-260	[»]
1YO2	X-ray	1.80	A	2-260	[»]
1Z9Y	X-ray	1.66	A	2-260	[»]
1ZE8	X-ray	2.00	A	2-260	[»]
1ZFK	X-ray	1.56	A	2-260	[»]
1ZFQ	X-ray	1.55	A	2-260	[»]
1ZGE	X-ray	1.65	A	2-260	[»]
1ZGF	X-ray	1.75	A	2-260	[»]
1ZH9	X-ray	1.70	A	2-260	[»]
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	2-260	[»]
2AW1	X-ray	1.46	A	2-260	[»]
2AX2	X-ray	1.50	A	2-260	[»]
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	2-260	[»]
2EU3	X-ray	1.60	A	2-260	[»]
2EZ7	X-ray	2.00	A	2-260	[»]
2F14	X-ray	1.71	A	2-260	[»]
2FMG	X-ray	1.60	A	2-260	[»]
2FMZ	X-ray	1.60	A	2-260	[»]
2FNK	X-ray	1.80	A	2-260	[»]
2FNM	X-ray	1.80	A	2-260	[»]
2FNN	X-ray	1.80	A	2-260	[»]
2FOQ	X-ray	1.25	A	2-260	[»]
2FOS	X-ray	1.10	A	2-260	[»]
2FOU	X-ray	0.99	A	2-260	[»]
2FOV	X-ray	1.15	A	2-260	[»]
2GD8	X-ray	1.46	A	2-260	[»]
2GEH	X-ray	2.00	A	2-260	[»]
2H15	X-ray	1.90	A	2-260	[»]
2H4N	X-ray	1.90	A	2-260	[»]
2HD6	X-ray	1.80	A	2-260	[»]
2HKK	X-ray	1.90	A	2-260	[»]
2HL4	X-ray	1.55	A	2-260	[»]
2HNC	X-ray	1.55	A	2-260	[»]
2HOC	X-ray	2.10	A	2-260	[»]
2ILI	X-ray	1.05	A	2-260	[»]
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	2-260	[»]
2NWP	X-ray	1.80	A	2-260	[»]
2NWY	X-ray	1.65	A	2-260	[»]
2NWZ	X-ray	1.80	A	2-260	[»]
2NXR	X-ray	1.70	A	2-260	[»]
2NXS	X-ray	1.80	A	2-260	[»]
2NXT	X-ray	1.15	A	2-260	[»]
2O4Z	X-ray	2.10	A	2-260	[»]
2OSF	X-ray	1.60	A	2-260	[»]
2OSM	X-ray	1.60	A	2-260	[»]
2POU	X-ray	1.60	A	2-260	[»]
2POV	X-ray	1.60	A	2-260	[»]
2POW	X-ray	1.75	A	2-260	[»]
2Q1B	X-ray	1.70	A	2-260	[»]
2Q1Q	X-ray	1.90	A	2-260	[»]
2Q38	X-ray	1.95	A	2-260	[»]
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	2-260	[»]
2VVB	X-ray	1.66	X	2-260	[»]
2WD2	X-ray	1.49	A	2-260	[»]
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	2-260	[»]
3BET	X-ray	1.85	A	2-260	[»]
3BL0	X-ray	1.90	A	2-260	[»]
3BL1	X-ray	2.10	A	2-260	[»]
3C7P	X-ray	1.70	A	2-260	[»]
3CA2	X-ray	2.00	A	2-260	[»]
3CAJ	X-ray	1.80	A	2-260	[»]
3CYU	X-ray	1.70	A	2-260	[»]
3D8W	X-ray	1.70	A	2-260	[»]
3D92	X-ray	1.10	A	2-260	[»]
3D93	X-ray	1.10	A	2-260	[»]
3D9Z	X-ray	1.65	A	2-260	[»]
3DAZ	X-ray	1.60	A	2-260	[»]
3DBU	X-ray	1.70	A	2-260	[»]
3DC3	X-ray	1.70	A	2-260	[»]
3DC9	X-ray	1.60	A	2-260	[»]
3DCC	X-ray	1.60	A	2-260	[»]
3DCS	X-ray	1.80	A	2-260	[»]
3DCW	X-ray	1.50	A	2-260	[»]
3DD0	X-ray	1.48	A	2-260	[»]
3DD8	X-ray	1.90	A	2-260	[»]
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	[»]
3EFT	X-ray	1.85	A	1-260	[»]
3F4X	X-ray	1.90	A	2-260	[»]
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	[»]
3IQK	X-ray	1.20	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	[»]
3P25	X-ray	1.49	A	1-260	[»]
3P29	X-ray	1.49	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	[»]
3PO6	X-ray	1.47	A	2-260	[»]
3PYK	X-ray	1.30	A	3-260	[»]
3R16	X-ray	1.60	A	4-260	[»]
3R17	X-ray	1.70	B	4-260	[»]
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	[»]
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	[»]
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	[»]
4CA2	X-ray	2.10	A	2-260	[»]
4CAC	X-ray	2.20	A	2-260	[»]
5CA2	X-ray	2.10	A	2-260	[»]
5CAC	X-ray	2.20	A	2-260	[»]
6CA2	X-ray	2.50	A	2-260	[»]
7CA2	X-ray	2.40	A	2-260	[»]
8CA2	X-ray	2.40	A	2-260	[»]
9CA2	X-ray	2.80	A	2-260	[»]

ProteinModelPortal

P00918.

SMR

P00918. Positions 3-260.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00918. 4 interactions.

MINT

MINT-1367766.

STRING

P00918.

PTM databases

PhosphoSite

P00918.

Polymorphism databases

DMDM

115456.

2D gel databases

OGP

P00918.

REPRODUCTION-2DPAGE

IPI00218414.
P00918.

UCD-2DPAGE

P00918.

Proteomic databases

PeptideAtlas

P00918.

PRIDE

P00918.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000285379; ENSP00000285379; ENSG00000104267.

GeneID

760.

KEGG

hsa:760.

UCSC

uc003ydk.2. human.

Organism-specific databases

CTD

760.

GeneCards

GC08P086376.

H-InvDB

HIX0007628.

HGNC

HGNC:1373. CA2.

HPA

CAB010102.
HPA001550.

MIM

259730. phenotype.
611492. gene.

neXtProt

NX_P00918.

Orphanet

2785. Osteopetrosis with renal tubular acidosis.

PharmGKB

PA25989.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09276.

GeneTree

ENSGT00560000076828.

HOGENOM

HBG717384.

HOVERGEN

HBG002837.

InParanoid

P00918.

OMA

WRPCQPL.

OrthoDB

EOG4X97HR.

PhylomeDB

P00918.

Enzyme and pathway databases

BRENDA

4.2.1.1. 2681.

Gene expression databases

ArrayExpress

P00918.

Bgee

P00918.

CleanEx

HS_CA2.

Genevestigator

P00918.

GermOnline

ENSG00000104267. Homo sapiens.

Family and domain databases

InterPro

IPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018440. Carbonic_anhydrase_CA2.
[Graphical view]

Gene3D

G3DSA:3.10.200.10. Euk_COanhd. 1 hit.

KO

K01672.

PANTHER

PTHR18952:SF28. Carbonic_anhydrase_CA2. 1 hit.
PTHR18952. Euk_COanhd. 1 hit.

Pfam

PF00194. Carb_anhydrase. 1 hit.
[Graphical view]

SMART

SM01057. Carb_anhydrase. 1 hit.
[Graphical view]

SUPFAM

SSF51069. Euk_COanhd. 1 hit.

PROSITE

PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00918.

DrugBank

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.

NextBio

3074.

SOURCE

Search...

Entry information

Entry name

CAH2_HUMAN

Accession

Primary (citable) accession number: P00918
Secondary accession number(s): B2R7G8, Q6FI12, Q96ET9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 158 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.