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1TB0

Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

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
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
XHOH265

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
XALA65

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
XPHE95

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
XTRP97
XLEU120

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
ChainResidueDetails
XTHR200

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962
ChainResidueDetails
XGLY8

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
XGLY63
XVAL68

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
XPHE93

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139
ChainResidueDetails
XHIS3

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
XILE167
XALA174

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 216
ChainResidueDetails
XALA65hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
XPHE95metal ligand
XTRP97metal ligand
XHIS107activator, electrostatic stabiliser, hydrogen bond acceptor
XLEU120metal ligand
XTHR200activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

217705

PDB entries from 2024-03-27

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