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3U3A

structure of Human Carbonic Anhydrase II V143I

Functional Information from GO Data
ChainGOidnamespacecontents
X0002009biological_processmorphogenesis of an epithelium
X0004064molecular_functionarylesterase activity
X0004089molecular_functioncarbonate dehydratase activity
X0005515molecular_functionprotein binding
X0005737cellular_componentcytoplasm
X0005829cellular_componentcytosol
X0005886cellular_componentplasma membrane
X0008270molecular_functionzinc ion binding
X0015670biological_processcarbon dioxide transport
X0016020cellular_componentmembrane
X0016829molecular_functionlyase activity
X0018820molecular_functioncyanamide hydratase activity
X0032230biological_processpositive regulation of synaptic transmission, GABAergic
X0032849biological_processpositive regulation of cellular pH reduction
X0038166biological_processangiotensin-activated signaling pathway
X0043209cellular_componentmyelin sheath
X0044070biological_processregulation of monoatomic anion transport
X0045177cellular_componentapical part of cell
X0046872molecular_functionmetal ion binding
X0046903biological_processsecretion
X0051453biological_processregulation of intracellular pH
X0070050biological_processneuron cellular homeostasis
X0070062cellular_componentextracellular exosome
X2001150biological_processpositive regulation of dipeptide transmembrane transport
X2001225biological_processregulation of chloride transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN X 262
ChainResidue
XHIS94
XHIS96
XHIS119
XHOH337

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL X 1304
ChainResidue
XTYR7
XASP243
XTRP245
XHOH434
XHOH461

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL X 263
ChainResidue
XGLN92
XPHE131
XHOH300
XHOH403
XHOH449

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
ChainResidueDetails
XSER105-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962
ChainResidueDetails
XHIS64

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:4621826, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
ChainResidueDetails
XHIS94

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
ChainResidueDetails
XHIS96
XHIS119

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
ChainResidueDetails
XTHR199

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962
ChainResidueDetails
XTYR7

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
ChainResidueDetails
XASN62
XASN67

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
ChainResidueDetails
XGLN92

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139
ChainResidueDetails
XSER2

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
XSER166
XSER173

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 216
ChainResidueDetails

237735

PDB entries from 2025-06-18

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