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6T5P

Human Carbonic anhydrase XII bound by 3,5-Di-tert-butylbenzenesulfonamide

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
AVD8302

site_idAC2
Number of Residues9
Detailsbinding site for residue VD8 A 302
ChainResidue
ALEU197
ATHR198
ATHR199
AZN301
AASN64
AGLN89
AHIS91
AHIS93
AHIS117

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS91
BHIS93
BHIS117
BVD8302

site_idAC4
Number of Residues10
Detailsbinding site for residue VD8 B 302
ChainResidue
BASN64
BGLN89
BHIS91
BHIS93
BHIS117
BLEU197
BTHR198
BTHR199
BZN301
BHOH464

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO B 303
ChainResidue
BTHR44
BGLY80
BLEU81
BTYR190
BARG192

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS91
CHIS93
CHIS117
CVD8302

site_idAC7
Number of Residues10
Detailsbinding site for residue VD8 C 302
ChainResidue
CASN64
CGLN89
CHIS91
CHIS93
CHIS117
CVAL119
CLEU197
CTHR198
CTHR199
CZN301

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO C 303
ChainResidue
CTRP4
CTYR19
CHOH477

site_idAC9
Number of Residues8
Detailsbinding site for residue EDO C 304
ChainResidue
CSER42
CTHR44
CLEU46
CGLY80
CTYR190
CARG192
CHOH432
CHOH447

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO C 305
ChainResidue
CLYS166
CTHR227
CALA228
CTYR230
CGLU241
CHOH498

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DHIS91
DHIS93
DHIS117
DVD8302

site_idAD3
Number of Residues10
Detailsbinding site for residue VD8 D 302
ChainResidue
DASN64
DGLN89
DHIS91
DHIS93
DHIS117
DLEU197
DTHR198
DTHR199
DZN301
DHOH441

site_idAD4
Number of Residues5
Detailsbinding site for residue EDO D 303
ChainResidue
DTHR44
DLEU46
DGLY80
DTYR190
DARG192

site_idAD5
Number of Residues2
Detailsbinding site for residue EDO D 304
ChainResidue
DASP156
DSER160

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
BHIS66
CHIS66
DHIS66
AHIS66

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

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

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

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