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4WW8

Crystal structure of human carbonic anhydrase isozyme XII with 4-Propylthiobenzenesulfonamide

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
AVD9305

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 302
ChainResidue
AHOH600
AASN64
AGLN89
AHIS91
AHOH547
AHOH583

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 303
ChainResidue
AASP156
ASER160
AHOH556

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 304
ChainResidue
AASN71
ALEU72
ATHR88
AHOH486
AHOH509

site_idAC5
Number of Residues9
Detailsbinding site for residue VD9 A 305
ChainResidue
AHIS91
AHIS93
AHIS117
AVAL119
ALEU197
ATHR198
ATHR199
ATRP208
AZN301

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS91
BHIS93
BHIS117
BVD9308

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO B 302
ChainResidue
BASN64
BGLN89
BHIS91
BEDO305
BHOH501
BHOH576

site_idAC8
Number of Residues6
Detailsbinding site for residue EDO B 303
ChainResidue
BSER42
BTHR44
BLEU46
BGLY80
BTYR190
BARG192

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO B 304
ChainResidue
BASP156
BSER160
BGLN221
BALA224
BHOH657

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO B 305
ChainResidue
BASN64
BLYS69
BGLN89
BEDO302
BVD9308
BHOH404

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO B 306
ChainResidue
BLEU183
BVAL215
BHOH493
BHOH508
BHOH622

site_idAD3
Number of Residues4
Detailsbinding site for residue EDO B 307
ChainResidue
BLEU256
BTYR258
BHOH522
BHOH595

site_idAD4
Number of Residues9
Detailsbinding site for residue VD9 B 308
ChainResidue
BHIS91
BHIS93
BHIS117
BLEU197
BTHR198
BTHR199
BTRP208
BZN301
BEDO305

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS91
CHIS93
CHIS117
CVD9304

site_idAD6
Number of Residues4
Detailsbinding site for residue EDO C 302
ChainResidue
CASN64
CGLN89
CHIS91
CHOH562

site_idAD7
Number of Residues6
Detailsbinding site for residue EDO C 303
ChainResidue
CASN71
CLEU72
CTHR88
CHOH489
CHOH512
CHOH518

site_idAD8
Number of Residues9
Detailsbinding site for residue VD9 C 304
ChainResidue
CHIS91
CHIS93
CHIS117
CVAL119
CLEU197
CTHR198
CTHR199
CTRP208
CZN301

site_idAD9
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DHIS91
DHIS93
DHIS117
DVD9304

site_idAE1
Number of Residues8
Detailsbinding site for residue EDO D 302
ChainResidue
DASN64
DHIS66
DGLN89
DHIS91
DVD9304
DHOH478
DHOH612
DHOH637

site_idAE2
Number of Residues6
Detailsbinding site for residue EDO D 303
ChainResidue
DSER42
DTHR44
DLEU46
DGLY80
DTYR190
DARG192

site_idAE3
Number of Residues10
Detailsbinding site for residue VD9 D 304
ChainResidue
DHIS91
DHIS93
DHIS117
DALA129
DLEU197
DTHR198
DTHR199
DTRP208
DZN301
DEDO302

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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