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3V3I

Kinetic and structural studies of thermostabilized mutants of HCA II.

Functional Information from GO Data
ChainGOidnamespacecontents
B0002009biological_processmorphogenesis of an epithelium
B0004064molecular_functionarylesterase activity
B0004089molecular_functioncarbonate dehydratase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006730biological_processone-carbon metabolic process
B0008270molecular_functionzinc ion binding
B0015670biological_processcarbon dioxide transport
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0018820molecular_functioncyanamide hydratase activity
B0032230biological_processpositive regulation of synaptic transmission, GABAergic
B0032849biological_processpositive regulation of cellular pH reduction
B0038166biological_processangiotensin-activated signaling pathway
B0043209cellular_componentmyelin sheath
B0044070biological_processregulation of monoatomic anion transport
B0045177cellular_componentapical part of cell
B0046872molecular_functionmetal ion binding
B0046903biological_processsecretion
B0051453biological_processregulation of intracellular pH
B0070050biological_processneuron cellular homeostasis
B0070062cellular_componentextracellular exosome
B2001150biological_processpositive regulation of dipeptide transmembrane transport
B2001225biological_processregulation of chloride transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119
BHOH410

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 302
ChainResidue
BGLN158
BGLU221

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
ChainResidueDetails
BSER105-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
BHIS64

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
BHIS94

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
BHIS96
BHIS119

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
ChainResidueDetails
BTHR199

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962
ChainResidueDetails
BPHE7

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
BASN62
BGLN67

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
BGLN92

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139
ChainResidueDetails
BSER2

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER166
BSER173

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 216
ChainResidueDetails
BHIS64hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS94metal ligand
BHIS96metal ligand
BGLU106activator, electrostatic stabiliser, hydrogen bond acceptor
BHIS119metal ligand
BTHR199activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

218853

PDB entries from 2024-04-24

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