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Entry version 259 (25 May 2022)
Sequence version 2 (23 Jan 2007)
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Protein

Carbonic anhydrase 2

Gene

CA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the reversible hydration of carbon dioxide (PubMed:1909891, PubMed:1910042, PubMed:1336460, PubMed:8485129, PubMed:8399159, PubMed:8218160, PubMed:8262987, PubMed:8451242, PubMed:7901850, PubMed:7761440, PubMed:8639494, PubMed:9265618, PubMed:17330962, PubMed:9398308, PubMed:11327835, PubMed:12056894, PubMed:17346964, PubMed:12171926, PubMed:15453828, PubMed:16214338, PubMed:15865431, PubMed:16106378, PubMed:15300855, PubMed:15667203, PubMed:18942852, PubMed:11831900, PubMed:17251017).

Can also hydrate cyanamide to urea (PubMed:10550681, PubMed:11015219).

Stimulates the chloride-bicarbonate exchange activity of SLC26A6 (PubMed:15990874).

Essential for bone resorption and osteoclast differentiation (PubMed:15300855).

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.

30 Publications

Miscellaneous

Target of drugs used in treatments against glaucoma disorder and breast cancer.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+22 Publications, Co2+1 PublicationNote: Zinc. Can also use cobalt(II) with lower efficiency, but not copper(II), nickel(II) and manganese(II).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=9.3 mM for CO22 Publications
  2. KM=11 mM for CO21 Publication
  3. KM=8.2 mM for CO21 Publication
  4. KM=82 mM for H2CO31 Publication
  5. KM=2.9 mM for 4-nitrophenyl acetate1 Publication

pH dependencei

Optimum pH is 6-8.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei7Fine-tunes the proton-transfer properties of H-641 Publication1
Sitei62Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine1 Publication2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei64Proton donor/acceptor2 Publications1
Sitei67Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine1 Publication2 Publications1
Sitei92Involved in the binding of some activators, including histamine and L-histidine1 Publication2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi94Zinc; catalytic23 Publications1
Metal bindingi96Zinc; catalytic22 Publications1
Metal bindingi119Zinc; catalytic22 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
4.2.1.1, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P00918

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1237044, Erythrocytes take up carbon dioxide and release oxygen
R-HSA-1247673, Erythrocytes take up oxygen and release carbon dioxide
R-HSA-1475029, Reversible hydration of carbon dioxide

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P00918

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P00918

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Carbonic anhydrase 2 (EC:4.2.1.17 Publications)
Alternative name(s):
Carbonate dehydratase II
Carbonic anhydrase C
Short name:
CAC
Carbonic anhydrase II
Short name:
CA-II
Cyanamide hydratase CA2Curated (EC:4.2.1.691 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CA2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:1373, CA2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
611492, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P00918

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000104267

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Osteopetrosis, autosomal recessive 3 (OPTB3)5 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_00138192Q → P in OPTB3; in Czechoslovakia. 2 PublicationsCorresponds to variant dbSNP:rs1304160279EnsemblClinVar.1
Natural variantiVAR_02100994H → Y in OPTB3; partial loss of activity. 1 Publication1
Natural variantiVAR_001382107H → Y in OPTB3. 4 PublicationsCorresponds to variant dbSNP:rs118203933EnsemblClinVar.1
Natural variantiVAR_021010144G → R in OPTB3; complete loss of activity. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi5W → A: Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with W-64. 1 Publication1
Mutagenesisi7Y → F: Enhanced activity. 2 Publications1
Mutagenesisi7Y → H: Reduced proton transfer rate. 2 Publications1
Mutagenesisi62N → A: Reduced activity. 1 Publication1
Mutagenesisi62N → D: Strongly reduced activity. 1 Publication1
Mutagenesisi62N → H: Reduced proton transfer; when associated with A-64. 3 Publications1
Mutagenesisi62N → L: Reduced activity. 2 Publications1
Mutagenesisi62N → T: Reduced activity. 1 Publication1
Mutagenesisi62N → V: Reduced activity. 1 Publication1
Mutagenesisi64H → 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 Publications1
Mutagenesisi64H → G: Impaired activity, not rescued by 4-methylimidazole (4-MI). 3 Publications1
Mutagenesisi64H → W: Impaired activity, rescued by 4-methylimidazole (4-MI). Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with A-5. 3 Publications1
Mutagenesisi65A → F: Reduced activity. 1
Mutagenesisi65A → S: 2-fold decrease in enzyme efficiency, as determined by kcat/KM ratio, and efficiently inhibited by chlorzolamide; when associated with Q-67. 1 Publication1
Mutagenesisi67N → H: Enhanced proton transfer; when associated with A-64. 1 Publication1
Mutagenesisi67N → L: Reduced activity. 1 Publication1
Mutagenesisi67N → Q: 2-fold decrease in enzyme efficiency, as determined by kcat/KM ratio, and efficiently inhibited by chlorzolamide; when associated with S-65. 1 Publication1
Mutagenesisi94H → C, D, E, N or Q: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities, impaired stability of zinc binding. 2 Publications1
Mutagenesisi106E → A or Q: Strongly reduced CO(2) hydrase activity. 2 Publications1
Mutagenesisi106E → D: Normal CO(2) hydrase activity. 2 Publications1
Mutagenesisi117E → Q: Strongly reduced activity and sulfonamide affinity. 1 Publication1
Mutagenesisi119H → D, N or Q: Reduced activity. 1 Publication1
Mutagenesisi119H → E: Strongly reduced activity. 1 Publication1
Mutagenesisi121V → A, G, I, L or S: Reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. 1 Publication1
Mutagenesisi121V → K or R: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. 1 Publication1
Mutagenesisi142V → F or Y: Strongly impaired activity. 1 Publication1
Mutagenesisi142V → G: Weakly impaired activity. 1 Publication1
Mutagenesisi142V → H: Impaired activity. 1 Publication1
Mutagenesisi197L → A: Reduced CO(2) hydrase activity. 1 Publication1
Mutagenesisi197L → E, H or R: Strongly reduced CO(2) hydrase activity. 1 Publication1
Mutagenesisi197L → F: Normal activity. 1 Publication1
Mutagenesisi198T → A, C, H or P: Strongly reduced activity. 5 Publications1
Mutagenesisi198T → D or E: Strongly reduced activity, but enhanced zinc affinity. 5 Publications1
Mutagenesisi198T → S or V: Reduced activity. 5 Publications1
Mutagenesisi199T → H: Higher affinity for bicarbonate. Enhanced proton transfer capacity; when associated with A-64. 3 Publications1
Mutagenesisi199T → S: Enhanced p-nitrophenyl acetate esterase activity, but normal CO(2) hydrase activity. 3 Publications1
Mutagenesisi201P → A: Normal CO(2) hydrase activity, but impaired stability. 1 Publication1

Keywords - Diseasei

Disease variant, Osteopetrosis

Organism-specific databases

DisGeNET

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DisGeNETi
760

MalaCards human disease database

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MalaCardsi
CA2
MIMi259730, phenotype

Open Targets

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OpenTargetsi
ENSG00000104267

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
2785, Osteopetrosis with renal tubular acidosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA25989

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P00918, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL205

Drug and drug target database

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DrugBanki
DB07596, (17beta)-17-(cyanomethyl)-2-methoxyestra-1(10),2,4-trien-3-yl sulfamate
DB03333, (4-sulfamoyl-phenyl)-thiocarbamic acid O-(2-thiophen-3-yl-ethyl) ester
DB08418, (4aS,4bR,10bS,12aS)-12a-methyl-1,3-dioxo-2-(pyridin-3-ylmethyl)-1,2,3,4,4a,4b,5,6,10b,11,12,12a-dodecahydronaphtho[2,1-f]isoquinolin-8-yl sulfamate
DB04081, (4s-Trans)-4-(Methylamino)-5,6-Dihydro-6-Methyl-4h-Thieno(2,3-B)Thiopyran-2-Sulfonamide-7,7-Dioxide
DB08416, (9BETA,13ALPHA,14BETA,17ALPHA)-2-METHOXYESTRA-1,3,5(10)-TRIENE-3,17-DIYL DISULFAMATE
DB02479, (R)-N-(3-Indol-1-Yl-2-Methyl-Propyl)-4-Sulfamoyl-Benzamide
DB07467, (S)-Indapamide
DB03950, (S)-N-(3-Indol-1-Yl-2-Methyl-Propyl)-4-Sulfamoyl-Benzamide
DB03594, 1,2,4-Triazole
DB03294, 1-Methyl-3-Oxo-1,3-Dihydro-Benzo[C]Isothiazole-5-Sulfonic Acid Amide
DB04763, 1-N-(4-SULFAMOYLPHENYL-ETHYL)-2,4,6-TRIMETHYLPYRIDINIUM
DB03270, 2,6-Difluorobenzenesulfonamide
DB08083, 2-(1,3-thiazol-4-yl)-1H-benzimidazole-5-sulfonamide
DB06954, 2-(cycloheptylmethyl)-1,1-dioxido-1-benzothiophen-6-yl sulfamate
DB08659, 2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
DB08046, 2-chloro-5-[(1S)-1-hydroxy-3-oxo-2H-isoindol-1-yl]benzenesulfonamide
DB02087, 3,5-Difluorobenzenesulfonamide
DB08156, 3-[4-(AMINOSULFONYL)PHENYL]PROPANOIC ACID
DB04203, 3-Mercuri-4-Aminobenzenesulfonamide
DB04394, 3-Nitro-4-(2-Oxo-Pyrrolidin-1-Yl)-Benzenesulfonamide
DB08782, 4-(2-AMINOETHYL)BENZENESULFONAMIDE
DB04549, 4-(Aminosulfonyl)-N-[(2,3,4-Trifluorophenyl)Methyl]-Benzamide
DB02221, 4-(Aminosulfonyl)-N-[(2,4,6-Trifluorophenyl)Methyl]-Benzamide
DB04180, 4-(Aminosulfonyl)-N-[(2,4-Difluorophenyl)Methyl]-Benzamide
DB03039, 4-(Aminosulfonyl)-N-[(2,5-Difluorophenyl)Methyl]-Benzamide
DB02861, 4-(Aminosulfonyl)-N-[(3,4,5-Trifluorophenyl)Methyl]-Benzamide
DB02429, 4-(Aminosulfonyl)-N-[(4-Fluorophenyl)Methyl]-Benzamide
DB08202, 4-({[(4-METHYLPIPERAZIN-1-YL)AMINO]CARBONOTHIOYL}AMINO)BENZENESULFONAMIDE
DB04600, 4-[(3-BROMO-4-O-SULFAMOYLBENZYL)(4-CYANOPHENYL)AMINO]-4H-[1,2,4]-TRIAZOLE
DB04601, 4-[(4-O-SULFAMOYLBENZYL)(4-CYANOPHENYL)AMINO]-4H-[1,2,4]-TRIAZOLE
DB01784, 4-Flourobenzenesulfonamide
DB03385, 4-Methylimidazole
DB03697, 4-Sulfonamide-[1-(4-Aminobutane)]Benzamide
DB04002, 4-Sulfonamide-[4-(Thiomethylaminobutane)]Benzamide
DB07632, 5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
DB07050, 5-[(phenylsulfonyl)amino]-1,3,4-thiadiazole-2-sulfonamide
DB06891, 5-{[(4-AMINO-3-CHLORO-5-FLUOROPHENYL)SULFONYL]AMINO}-1,3,4-THIADIAZOLE-2-SULFONAMIDE
DB08645, 6-CHLORO-3-(DICHLOROMETHYL)-3,4-DIHYDRO-2H-1,2,4-BENZOTHIADIAZINE-7-SULFONAMIDE 1,1-DIOXIDE
DB08765, 6-HYDROXY-1,3-BENZOTHIAZOLE-2-SULFONAMIDE
DB00819, Acetazolamide
DB03877, AL-4623
DB03262, Al-6619, [2h-Thieno[3,2-E]-1,2-Thiazine-6-Sulfonamide,2-(3-Hydroxyphenyl)-3-(4-Morpholinyl)-, 1,1-Dioxide]
DB03598, Al-6629, [2h-Thieno[3,2-E]-1,2-Thiazine-6-Sulfonamide,2-(3-Methoxyphenyl)-3-(4-Morpholinyl)-, 1,1-Dioxide]
DB04089, AL5300
DB01964, AL5424
DB03526, AL5927
DB04371, AL6528
DB02220, AL7089A
DB03221, AL7099A
DB02602, AL7182
DB02535, Aminodi(Ethyloxy)Ethylaminocarbonylbenzenesulfonamide
DB00436, Bendroflumethiazide
DB00562, Benzthiazide
DB01194, Brinzolamide
DB00482, Celecoxib
DB00880, Chlorothiazide
DB02679, Cyanamide
DB00606, Cyclothiazide
DB02866, Dansylamide
DB01119, Diazoxide
DB01144, Diclofenamide
DB00869, Dorzolamide
DB08846, Ellagic acid
DB01031, Ethinamate
DB00311, Ethoxzolamide
DB08157, ETHYL 3-[4-(AMINOSULFONYL)PHENYL]PROPANOATE
DB01942, Formic acid
DB00695, Furosemide
DB00774, Hydroflumethiazide
DB08165, indane-5-sulfonamide
DB02292, Irosustat
DB03975, Mercuribenzoic Acid
DB00703, Methazolamide
DB00232, Methyclothiazide
DB02610, N-(2,3,4,5,6-Pentaflouro-Benzyl)-4-Sulfamoyl-Benzamide
DB07742, N-(2,3-DIFLUORO-BENZYL)-4-SULFAMOYL-BENZAMIDE
DB03844, N-(2,6-Diflouro-Benzyl)-4-Sulfamoyl-Benzamide
DB02069, N-(2-Flouro-Benzyl)-4-Sulfamoyl-Benzamide
DB02986, N-(2-Thienylmethyl)-2,5-Thiophenedisulfonamide
DB08301, N-({[4-(AMINOSULFONYL)PHENYL]AMINO}CARBONYL)-4-METHYLBENZENESULFONAMIDE
DB07048, N-[(2R)-5-(aminosulfonyl)-2,3-dihydro-1H-inden-2-yl]-2-propylpentanamide
DB03596, N-[2-(1h-Indol-5-Yl)-Butyl]-4-Sulfamoyl-Benzamide
DB07476, N-[4-(AMINOSULFONYL)PHENYL]-2-MERCAPTOBENZAMIDE
DB01748, N-Benzyl-4-Sulfamoyl-Benzamide
DB08155, N-{2-[4-(AMINOSULFONYL)PHENYL]ETHYL}ACETAMIDE
DB01671, p-Hydroxymercuribenzoic acid
DB07710, PHENYLALANYLAMINODI(ETHYLOXY)ETHYL BENZENESULFONAMIDEAMINOCARBONYLBENZENESULFONAMIDE
DB01325, Quinethazone
DB09460, Sodium carbonate
DB09472, Sodium sulfate
DB02894, Sulfamic Acid 2,3-O-(1-Methylethylidene)-4,5-O-Sulfonyl-Beta-Fructopyranose Ester
DB00391, Sulpiride
DB08329, Sulthiame
DB07363, THIOPHENE-2,5-DISULFONIC ACID 2-AMIDE-5-(4-METHYL-BENZYLAMIDE)
DB00273, Topiramate
DB01021, Trichlormethiazide
DB03904, Urea
DB00580, Valdecoxib
DB14533, Zinc chloride
DB14548, Zinc sulfate, unspecified form
DB00909, Zonisamide

DrugCentral

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DrugCentrali
P00918

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
3092

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CA2

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000774182 – 260Carbonic anhydrase 2Add BLAST259

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine2 Publications1
Modified residuei2PhosphoserineBy similarity1
Modified residuei165PhosphoserineCombined sources1
Modified residuei172PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
CPTAC-177
CPTAC-178

Encyclopedia of Proteome Dynamics

More...
EPDi
P00918

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P00918

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P00918

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P00918

PeptideAtlas

More...
PeptideAtlasi
P00918

PRoteomics IDEntifications database

More...
PRIDEi
P00918

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
51292

2D gel databases

USC-OGP 2-DE database

More...
OGPi
P00918

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00218414
P00918

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
P00918

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P00918, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00918

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P00918

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000104267, Expressed in colonic mucosa and 227 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P00918, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P00918, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000104267, Tissue enhanced (intestine, stomach)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with SLC4A4 (PubMed:14567693, PubMed:15218065). Interaction with SLC4A7 regulates SLC4A7 transporter activity (PubMed:14736710).

Interacts with SLC26A6 isoform 4 (via C-terminus cytoplasmic domain) (PubMed:15990874).

4 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
107215, 41 interactors

Protein interaction database and analysis system

More...
IntActi
P00918, 14 interactors

Molecular INTeraction database

More...
MINTi
P00918

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000285379

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00918

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P00918, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P00918

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P00918

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00918

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini3 – 259Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST257

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni198 – 199Substrate binding2 Publications2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0382, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000160385

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_039326_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00918

Identification of Orthologs from Complete Genome Data

More...
OMAi
SADFPNF

Database of Orthologous Groups

More...
OrthoDBi
1377476at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00918

TreeFam database of animal gene trees

More...
TreeFami
TF316425

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.200.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001148, CA_dom
IPR036398, CA_dom_sf
IPR023561, Carbonic_anhydrase_a-class
IPR018338, Carbonic_anhydrase_a-class_CS

The PANTHER Classification System

More...
PANTHERi
PTHR18952, PTHR18952, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00194, Carb_anhydrase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01057, Carb_anhydrase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51069, SSF51069, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00162, ALPHA_CA_1, 1 hit
PS51144, ALPHA_CA_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P00918-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS
60 70 80 90 100
YDQATSLRIL NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL
110 120 130 140 150
DGQGSEHTVD KKKYAAELHL VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG
160 170 180 190 200
SAKPGLQKVV DVLDSIKTKG KSADFTNFDP RGLLPESLDY WTYPGSLTTP
210 220 230 240 250
PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM VDNWRPAQPL
260
KNRQIKASFK
Length:260
Mass (Da):29,246
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2EC2BB7548F10558
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RID5E5RID5_HUMAN
Carbonic anhydrase 2
CA2
97Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RK37E5RK37_HUMAN
Carbonic anhydrase 2
CA2
101Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti179 – 180DP → AA in AAH11949 (PubMed:15489334).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00138018K → E in Jogjakarta. 1 PublicationCorresponds to variant dbSNP:rs118203931EnsemblClinVar.1
Natural variantiVAR_00138192Q → P in OPTB3; in Czechoslovakia. 2 PublicationsCorresponds to variant dbSNP:rs1304160279EnsemblClinVar.1
Natural variantiVAR_02100994H → Y in OPTB3; partial loss of activity. 1 Publication1
Natural variantiVAR_001382107H → Y in OPTB3. 4 PublicationsCorresponds to variant dbSNP:rs118203933EnsemblClinVar.1
Natural variantiVAR_021010144G → R in OPTB3; complete loss of activity. 1 Publication1
Natural variantiVAR_001383236P → H in Melbourne. 1 PublicationCorresponds to variant dbSNP:rs118203932EnsemblClinVar.1
Natural variantiVAR_001384252N → D. Corresponds to variant dbSNP:rs2228063EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M77181 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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS6239.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A27175, CRHU2

NCBI Reference Sequences

More...
RefSeqi
NP_000058.1, NM_000067.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000285379.10; ENSP00000285379.4; ENSG00000104267.10

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
760

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:760

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...
MANE-Selecti
ENST00000285379.10; ENSP00000285379.4; NM_000067.3; NP_000058.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77181 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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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-ray0.90A