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5MSB

Crystal structure of human carbonic anhydrase isozyme XII with 2,3,5,6-tetrafluoro-4[(2-hydroxyethyl)sulfonyl]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
AHIS91
AHIS93
AHIS117
AV13303

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 302
ChainResidue
AGLU147
APRO214
AGLN216
AHOH416
AHOH458

site_idAC3
Number of Residues15
Detailsbinding site for residue V13 A 303
ChainResidue
AGLN89
AHIS91
AHIS93
AHIS117
AVAL119
ALEU139
AVAL141
ALEU197
ATHR198
ATHR199
ATRP208
AZN301
AHOH552
AHOH580
AHOH625

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS91
BHIS93
BHIS117
BV13305

site_idAC5
Number of Residues7
Detailsbinding site for residue PEG B 302
ChainResidue
BVAL107
BGLN110
BHIS111
BPHE112
BHOH409
BHOH529
BHOH581

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO B 303
ChainResidue
APHE7
AASN244
AHOH572
BLYS251
BASP253
BHOH406
BHOH487

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO B 304
ChainResidue
BARG212
BASN213

site_idAC8
Number of Residues18
Detailsbinding site for residue V13 B 305
ChainResidue
BGLN89
BHIS91
BHIS93
BHIS117
BVAL119
BALA129
BLEU139
BVAL141
BLEU197
BTHR198
BTHR199
BPRO200
BPRO201
BTRP208
BZN301
BHOH407
BHOH503
BHOH606

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS91
CHIS93
CHIS117
CV13302

site_idAD1
Number of Residues14
Detailsbinding site for residue V13 C 302
ChainResidue
CGLN89
CHIS91
CHIS93
CHIS117
CVAL119
CLEU139
CVAL141
CLEU197
CTHR198
CTHR199
CTRP208
CZN301
CHOH560
CHOH567

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DHIS91
DHIS93
DHIS117
DV13305

site_idAD3
Number of Residues6
Detailsbinding site for residue EDO D 302
ChainResidue
DSER42
DTHR44
DGLY80
DTYR190
DARG192
DHOH569

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO D 303
ChainResidue
DLEU43
DARG192
DHOH569

site_idAD5
Number of Residues7
Detailsbinding site for residue EDO D 304
ChainResidue
DHOH527
DSER133
DASN134
DPRO201
DASN203
DHOH430
DHOH452

site_idAD6
Number of Residues16
Detailsbinding site for residue V13 D 305
ChainResidue
DGLN89
DHIS91
DHIS93
DHIS117
DVAL119
DALA129
DSER130
DLEU139
DVAL141
DLEU197
DTHR198
DTHR199
DTRP208
DZN301
DHOH422
DHOH577

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

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