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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1XEV

Crystal structure of human carbonic anhydrase II in a new crystal form

Functional Information from GO Data
ChainGOidnamespacecontents
A0002009biological_processmorphogenesis of an epithelium
A0004064molecular_functionarylesterase activity
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008270molecular_functionzinc ion binding
A0015670biological_processcarbon dioxide transport
A0016829molecular_functionlyase activity
A0018820molecular_functioncyanamide hydratase activity
A0032230biological_processpositive regulation of synaptic transmission, GABAergic
A0032849biological_processpositive regulation of cellular pH reduction
A0038166biological_processangiotensin-activated signaling pathway
A0043209cellular_componentmyelin sheath
A0044070biological_processregulation of monoatomic anion transport
A0045177cellular_componentapical part of cell
A0046872molecular_functionmetal ion binding
A0046903biological_processsecretion
A0051453biological_processregulation of intracellular pH
A0070050biological_processneuron cellular homeostasis
A0070062cellular_componentextracellular exosome
A2001150biological_processpositive regulation of dipeptide transmembrane transport
A2001225biological_processregulation of chloride transport
B0002009biological_processmorphogenesis of an epithelium
B0004064molecular_functionarylesterase activity
B0004089molecular_functioncarbonate dehydratase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008270molecular_functionzinc ion binding
B0015670biological_processcarbon dioxide transport
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
C0002009biological_processmorphogenesis of an epithelium
C0004064molecular_functionarylesterase activity
C0004089molecular_functioncarbonate dehydratase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0008270molecular_functionzinc ion binding
C0015670biological_processcarbon dioxide transport
C0016829molecular_functionlyase activity
C0018820molecular_functioncyanamide hydratase activity
C0032230biological_processpositive regulation of synaptic transmission, GABAergic
C0032849biological_processpositive regulation of cellular pH reduction
C0038166biological_processangiotensin-activated signaling pathway
C0043209cellular_componentmyelin sheath
C0044070biological_processregulation of monoatomic anion transport
C0045177cellular_componentapical part of cell
C0046872molecular_functionmetal ion binding
C0046903biological_processsecretion
C0051453biological_processregulation of intracellular pH
C0070050biological_processneuron cellular homeostasis
C0070062cellular_componentextracellular exosome
C2001150biological_processpositive regulation of dipeptide transmembrane transport
C2001225biological_processregulation of chloride transport
D0002009biological_processmorphogenesis of an epithelium
D0004064molecular_functionarylesterase activity
D0004089molecular_functioncarbonate dehydratase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0008270molecular_functionzinc ion binding
D0015670biological_processcarbon dioxide transport
D0016829molecular_functionlyase activity
D0018820molecular_functioncyanamide hydratase activity
D0032230biological_processpositive regulation of synaptic transmission, GABAergic
D0032849biological_processpositive regulation of cellular pH reduction
D0038166biological_processangiotensin-activated signaling pathway
D0043209cellular_componentmyelin sheath
D0044070biological_processregulation of monoatomic anion transport
D0045177cellular_componentapical part of cell
D0046872molecular_functionmetal ion binding
D0046903biological_processsecretion
D0051453biological_processregulation of intracellular pH
D0070050biological_processneuron cellular homeostasis
D0070062cellular_componentextracellular exosome
D2001150biological_processpositive regulation of dipeptide transmembrane transport
D2001225biological_processregulation of chloride transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 262
ChainResidue
AHIS94
AHIS96
AHIS119
AHOH395
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 562
ChainResidue
BHIS94
BHIS96
BHIS119
BHOH713
site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 862
ChainResidue
CHIS96
CHIS119
CHOH1031
CHIS94
site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 999
ChainResidue
DHIS94
DHIS96
DHIS119
DHOH1140
Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
ChainResidueDetails
ASER105-VAL121
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1024
DetailsDomain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15667203","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11076507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12499545","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1336460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1433293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1909891","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19583303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151020","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4621826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7803386","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7901850","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8218160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8262987","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8399159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8431430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8451242","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8482389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8639494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8987974","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9865942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11076507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12499545","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1336460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1433293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1909891","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19583303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151020","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7803386","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7901850","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8218160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8262987","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8399159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8431430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8451242","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8482389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8639494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8987974","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9865942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10550681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19520834","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Fine-tunes the proton-transfer properties of H-64","evidences":[{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsSite: {"description":"Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine","evidences":[{"source":"PubMed","id":"16214338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9265618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsSite: {"description":"Involved in the binding of some activators, including histamine and L-histidine","evidences":[{"source":"PubMed","id":"16214338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9265618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P27139","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR199
AHIS64
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
BTHR199
BHIS64
site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
CTHR199
CHIS64
site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
DTHR199
DHIS64
site_idMCSA1
Number of Residues6
DetailsM-CSA 216
ChainResidueDetails
AHIS64hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS94metal ligand
AHIS96metal ligand
AGLU106activator, electrostatic stabiliser, hydrogen bond acceptor
AHIS119metal ligand
ATHR199activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity
site_idMCSA2
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
site_idMCSA3
Number of Residues6
DetailsM-CSA 216
ChainResidueDetails
CHIS64hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
CHIS94metal ligand
CHIS96metal ligand
CGLU106activator, electrostatic stabiliser, hydrogen bond acceptor
CHIS119metal ligand
CTHR199activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity
site_idMCSA4
Number of Residues6
DetailsM-CSA 216
ChainResidueDetails
DHIS64hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
DHIS94metal ligand
DHIS96metal ligand
DGLU106activator, electrostatic stabiliser, hydrogen bond acceptor
DHIS119metal ligand
DTHR199activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

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PDB entries from 2025-10-29

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