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3TVN

Human Carbonic Anhydrase II Proton Transfer Mutant

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
X0006730biological_processone-carbon metabolic process
X0008270molecular_functionzinc ion binding
X0015670biological_processcarbon dioxide transport
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
XHOH394

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
XGLN67

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

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 216
ChainResidueDetails
XHIS64hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
XHIS94metal ligand
XHIS96metal ligand
XGLU106activator, electrostatic stabiliser, hydrogen bond acceptor
XHIS119metal ligand
XTHR199activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

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PDB entries from 2024-10-30

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