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6G5L

Crystal structure of human carbonic anhydrase isozyme XII with 4-chloro-2-(cyclohexylamino)-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
AEM5302

site_idAC2
Number of Residues19
Detailsbinding site for residue EM5 A 302
ChainResidue
AHIS93
AHIS117
AALA129
AVAL141
ALEU197
ATHR198
ATHR199
ATRP208
AZN301
APEG304
AHOH401
AHOH405
AHOH414
AHOH538
ATRP4
AASN64
AHIS66
AGLN89
AHIS91

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 303
ChainResidue
AASN134
ASER136
APRO204
AHOH404

site_idAC4
Number of Residues6
Detailsbinding site for residue PEG A 304
ChainResidue
ASER133
APRO201
AASN203
AEM5302
AHOH414
AHOH552

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 305
ChainResidue
AGLY50
AASN52
ALEU53
AASP75
BGLN49

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS91
BHIS93
BHIS117
BEM5302

site_idAC7
Number of Residues18
Detailsbinding site for residue EM5 B 302
ChainResidue
BASN64
BHIS66
BGLN89
BHIS91
BHIS93
BHIS117
BALA129
BSER130
BVAL141
BLEU197
BTHR198
BTHR199
BTRP208
BZN301
BEDO306
BHOH404
BHOH408
BHOH569

site_idAC8
Number of Residues7
Detailsbinding site for residue EDO B 303
ChainResidue
BLEU183
BPRO184
BGLU185
BVAL215
BHOH414
BHOH502
BHOH544

site_idAC9
Number of Residues9
Detailsbinding site for residue EDO B 304
ChainResidue
BSER42
BTHR44
BLEU46
BGLY80
BLEU81
BTYR190
BARG192
BHOH409
BHOH578

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO B 305
ChainResidue
BARG255
BLEU256
BTYR258
BHOH510
BHOH564

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO B 306
ChainResidue
BASN64
BLYS69
BGLN89
BEM5302
BHOH453

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS91
CHIS93
CHIS117
CEM5302

site_idAD4
Number of Residues15
Detailsbinding site for residue EM5 C 302
ChainResidue
CTRP208
CZN301
CHOH441
CHOH478
CHOH522
CHOH562
CGLN89
CHIS91
CHIS93
CHIS117
CALA129
CVAL141
CLEU197
CTHR198
CTHR199

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO C 303
ChainResidue
CPRO201
CASN203
CHOH406
CHOH510
CHOH546

site_idAD6
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DHIS91
DHIS93
DHIS117
DEM5302

site_idAD7
Number of Residues13
Detailsbinding site for residue EM5 D 302
ChainResidue
DTRP4
DGLN89
DHIS91
DHIS93
DHIS117
DVAL141
DLEU197
DTHR198
DTHR199
DTRP208
DZN301
DHOH425
DHOH539

site_idAD8
Number of Residues5
Detailsbinding site for residue EDO D 303
ChainResidue
DHIS33
DSER34
DSER108
DHOH427
DHOH586

site_idAD9
Number of Residues7
Detailsbinding site for residue EDO D 304
ChainResidue
DSER42
DTHR44
DLEU46
DGLY80
DTYR190
DARG192
DHOH499

site_idAE1
Number of Residues4
Detailsbinding site for residue EDO D 305
ChainResidue
DASN134
DASN203
DHOH403
DHOH505

site_idAE2
Number of Residues6
Detailsbinding site for residue EDO D 306
ChainResidue
AGLU171
APHE173
DHIS164
DALA172
DPHE173
DHOH424

site_idAE3
Number of Residues7
Detailsbinding site for residue PEG D 307
ChainResidue
DLEU26
DARG194
DARG255
DLEU256
DTYR258
DHOH480
DHOH532

site_idAE4
Number of Residues5
Detailsbinding site for residue EDO D 308
ChainResidue
DLYS251
DPHE252
DASP253
DHOH402
DHOH461

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
DHIS91
DHIS93
DHIS117
AHIS93
AHIS117
BHIS91
BHIS93
BHIS117
CHIS91
CHIS93
CHIS117

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

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PDB entries from 2024-07-17

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