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4HT2

Crystal structure of human carbonic anhydrase isozyme XII with the inhibitor.

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
AV50302

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE V50 A 302
ChainResidue
ASER130
ALEU139
AVAL141
ALEU197
ATHR198
ATHR199
APRO200
AASN203
ATRP208
AZN301
APEG303
AEDO304
AHOH543
AHOH592
AHOH604
AGLN89
AHIS91
AHIS93
AHIS117
AVAL119

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG A 303
ChainResidue
AASN64
ALYS69
AGLN89
ATHR199
AV50302
AEDO304

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AASN64
ASER67
AGLN89
AHIS91
AHIS93
ATHR199
AV50302
APEG303
AHOH498

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
ASER42
ALEU43
ATHR44
AGLY80
ATYR190
AARG192

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
AASP40
ATYR258
AHOH488

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS91
BHIS93
BHIS117
BV50302

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE V50 B 302
ChainResidue
BGLN89
BHIS91
BHIS93
BHIS117
BVAL119
BSER133
BLEU197
BTHR198
BTHR199
BPRO200
BZN301
BEDO304
BEDO305
BHOH492

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PEG B 303
ChainResidue
BHIS164
BPHE173
BHOH499
BHOH573
BHOH769
CGLN58
CHIS161
CPHE173
CPRO175

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 304
ChainResidue
BASN64
BHIS66
BGLN89
BHIS91
BV50302
BEDO305
BHOH450
BHOH642

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 305
ChainResidue
BASN64
BLYS69
BV50302
BEDO304
BHOH641
BHOH648

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 306
ChainResidue
BASN71
BLEU72
BTHR88
BHOH437
BHOH445
BHOH456

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 307
ChainResidue
BSER83
BASP124
BMET234
BASP235

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 308
ChainResidue
BLYS57
BGLN58
BHOH617
CHIS164

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 301
ChainResidue
CHIS91
CHIS93
CHIS117
CV50302

site_idBC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE V50 C 302
ChainResidue
CGLN89
CHIS91
CHIS93
CHIS117
CVAL119
CSER133
CLEU139
CLEU197
CTHR198
CTHR199
CPRO200
CPRO201
CTRP208
CZN301
CEDO303
CHOH608

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 303
ChainResidue
CASN64
CHIS66
CGLN89
CHIS91
CV50302
CHOH609
CHOH611

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
DHIS91
DHIS93
DHIS117
DV50302

site_idCC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE V50 D 302
ChainResidue
DGLN89
DHIS91
DHIS93
DHIS117
DVAL119
DSER133
DLEU197
DTHR198
DTHR199
DPRO200
DZN301
DEDO304
DEDO305
DHOH662

site_idCC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PEG D 303
ChainResidue
DGLN163
DGLU220
DALA224
DHOH531
DHOH551
DHOH582
DHOH606
DHOH626
DHOH786

site_idCC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO D 304
ChainResidue
DASN64
DHIS66
DSER67
DGLN89
DHIS91
DV50302
DEDO305
DHOH664

site_idCC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO D 305
ChainResidue
DASN64
DLYS69
DGLN89
DV50302
DEDO304
DHOH663
DHOH665

site_idCC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO D 306
ChainResidue
AALA55
APRO175
AHOH677
AHOH728
AHOH729
DSER160
DHIS161
DHIS164

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 2024-07-24

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