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6FE1

Three dimensional structure of human carbonic anhydrase IX in complex with benzenesulfonamide.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0008270molecular_functionzinc ion binding
B0004089molecular_functioncarbonate dehydratase activity
B0008270molecular_functionzinc ion binding
C0004089molecular_functioncarbonate dehydratase activity
C0008270molecular_functionzinc ion binding
D0004089molecular_functioncarbonate dehydratase activity
D0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS94
AHIS96
AHIS119
AV14302

site_idAC2
Number of Residues12
Detailsbinding site for residue V14 A 302
ChainResidue
AGLU106
AHIS119
AVAL121
ALEU198
ATHR199
ATHR200
AZN301
AASN62
AGLN67
AGLN92
AHIS94
AHIS96

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119
BV14302

site_idAC4
Number of Residues11
Detailsbinding site for residue V14 B 302
ChainResidue
BASN62
BHIS64
BGLN92
BHIS94
BHIS96
BGLU106
BHIS119
BVAL131
BLEU198
BTHR199
BZN301

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS94
CHIS96
CHIS119
CV14302

site_idAC6
Number of Residues13
Detailsbinding site for residue V14 C 302
ChainResidue
CASN62
CGLN67
CGLN92
CHIS94
CHIS96
CGLU106
CHIS119
CVAL121
CVAL131
CLEU198
CTHR199
CTHR200
CZN301

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DHIS94
DHIS96
DHIS119
DV14302

site_idAC8
Number of Residues13
Detailsbinding site for residue V14 D 302
ChainResidue
DASN62
DHIS64
DGLN67
DHIS94
DHIS96
DGLU106
DHIS119
DVAL121
DVAL131
DLEU198
DTHR199
DTHR200
DZN301

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19805286","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18703501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19805286","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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