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6SKT

Crystal structure of bovine carbonic anhydrase II in complex with a benzenesulfonamide-based ligand (SH0)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0008270molecular_functionzinc ion binding
A0018820molecular_functioncyanamide hydratase activity
A0038166biological_processangiotensin-activated signaling pathway
A0044070biological_processregulation of monoatomic anion transport
A0045177cellular_componentapical part of cell
A0051453biological_processregulation of intracellular pH
A2001150biological_processpositive regulation of dipeptide transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CU A 1001
ChainResidue
AHIS4
AHIS10
AHIS15
AASP19

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1002
ChainResidue
AHIS94
AHIS96
AHIS119
AE6B1004

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 1003
ChainResidue
ASER65
AASN67
AGLN92
AHIS94
AHOH1107
AHOH1134
AASN62

site_idAC4
Number of Residues12
Detailsbinding site for residue E6B A 1004
ChainResidue
AHIS94
AHIS96
AHIS119
APHE130
APRO154
ALEU197
ATHR198
ATHR199
ATRP208
AZN1002
AHOH1121
AHOH1151

site_idAC5
Number of Residues4
Detailsbinding site for residue CU A 1005
ChainResidue
AHIS3
ATRP5
AHIS64
AHOH1130

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdrkkYaaELHLV
ChainResidueDetails
ASER105-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues256
DetailsDomain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15039588","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsSite: {"description":"Fine-tunes the proton-transfer properties of H-64","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

254587

PDB entries from 2026-06-03

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