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4Q0L

Crystal structure of catalytic domain of human carbonic anhydrase isozyme XII with inhibitor

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
AHIS91
AHIS93
AHIS117
AV14302

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE V14 A 302
ChainResidue
AHIS117
AVAL119
ASER133
ALEU197
ATHR198
ATHR199
AZN301
AASN64
ALYS69
AGLN89
AHIS91
AHIS93

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS91
BHIS93
BGLU104
BHIS117
BV14302

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE V14 B 302
ChainResidue
BTRP4
BASN64
BGLN89
BHIS91
BHIS93
BGLU104
BHIS117
BVAL119
BSER133
BLEU197
BTHR198
BTHR199
BZN301

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 301
ChainResidue
CHIS91
CHIS93
CHIS117
CV14302

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE V14 C 302
ChainResidue
CASN64
CLYS69
CGLN89
CHIS91
CHIS93
CGLU104
CHIS117
CVAL119
CSER133
CLEU197
CTHR198
CTHR199
CZN301

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
DHIS91
DHIS93
DGLU104
DHIS117
DV14302

site_idAC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE V14 D 302
ChainResidue
DASN64
DLYS69
DGLN89
DHIS91
DHIS93
DGLU104
DHIS117
DVAL119
DALA129
DSER133
DLEU197
DTHR198
DTHR199
DPRO200
DZN301

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVsgqhFaaELHIV
ChainResidueDetails
ASER103-VAL119

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":"11493685","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 Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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