Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS66
BHIS66
CHIS66
DHIS66

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:11493685
ChainResidueDetails
AHIS91
AHIS93
AHIS117
BHIS91
BHIS93
BHIS117
CHIS91
CHIS93
CHIS117
DHIS91
DHIS93
DHIS117

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR198
BTHR198
CTHR198
DTHR198

site_idSWS_FT_FI4
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN52
AASN134
BASN52
BASN134
CASN52
CASN134
DASN52
DASN134

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon