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6G7A

Crystal structure of human carbonic anhydrase isozyme XII 2-(benzylamino)-4-chloro-N-(2-hydroxyethyl)-5-sulfamoyl-benzamide

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
AEOQ303

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 302
ChainResidue
AASP156
ASER160
AHOH447

site_idAC3
Number of Residues17
Detailsbinding site for residue EOQ A 303
ChainResidue
AGLN89
AHIS91
AHIS93
AHIS117
ASER130
AVAL141
ALEU197
ATHR198
ATHR199
ATRP208
AZN301
AHOH407
AHOH412
AHOH426
AHOH500
ATRP4
AASN64

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS91
BHIS93
BHIS117
BEOQ305

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO B 302
ChainResidue
BTHR44
BLEU46
BGLY80
BTYR190
BARG192
BHOH423
BHOH601

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO B 303
ChainResidue
BASP156
BSER160
BGLN221
BALA224
BHOH519

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO B 304
ChainResidue
BLYS57
BGLN58
BHOH404
BHOH632

site_idAC8
Number of Residues15
Detailsbinding site for residue EOQ B 305
ChainResidue
BASN64
BGLN89
BHIS91
BHIS93
BHIS117
BSER130
BSER133
BVAL141
BLEU197
BTHR198
BTHR199
BTRP208
BZN301
BHOH403
BHOH581

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS91
CHIS93
CHIS117
CEOQ305

site_idAD1
Number of Residues8
Detailsbinding site for residue EDO C 302
ChainResidue
CSER42
CLEU46
CGLY80
CLEU81
CTYR190
CARG192
CHOH418
CHOH445

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO C 303
ChainResidue
CLEU46
CGLU47
CPHE48
CGLU180

site_idAD3
Number of Residues6
Detailsbinding site for residue EDO C 304
ChainResidue
CASN71
CLEU72
CTHR88
CHOH433
CHOH439
CHOH527

site_idAD4
Number of Residues17
Detailsbinding site for residue EOQ C 305
ChainResidue
CTRP4
CASN64
CGLN89
CHIS91
CHIS93
CHIS117
CVAL119
CSER130
CSER133
CVAL141
CLEU197
CTHR198
CTHR199
CTRP208
CZN301
CHOH403
CHOH548

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DHIS93
DHIS117
DEOQ307
DHIS91

site_idAD6
Number of Residues6
Detailsbinding site for residue EDO D 302
ChainResidue
DSER42
DTHR44
DLEU46
DGLY80
DTYR190
DARG192

site_idAD7
Number of Residues6
Detailsbinding site for residue EDO D 303
ChainResidue
DGLN110
DHIS111
DPHE112
DEDO304
DHOH417
DHOH612

site_idAD8
Number of Residues6
Detailsbinding site for residue EDO D 304
ChainResidue
DPHE112
DALA113
DGLU147
DMET148
DEDO303
DHOH508

site_idAD9
Number of Residues4
Detailsbinding site for residue EDO D 305
ChainResidue
DPRO100
DHIS101
DMET148
DHOH508

site_idAE1
Number of Residues3
Detailsbinding site for residue EDO D 306
ChainResidue
DASP156
DSER160
DHOH541

site_idAE2
Number of Residues15
Detailsbinding site for residue EOQ D 307
ChainResidue
DASN64
DGLN89
DHIS91
DHIS93
DHIS117
DSER130
DSER133
DVAL141
DLEU197
DTHR198
DTHR199
DTRP208
DZN301
DHOH402
DHOH544

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 Residues777
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":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11493685","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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