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6I0J

Crystal structure of human carbonic anhydrase I in complex with the 4-({[4-chloro-3-(trifluoromethyl)phenyl]carbamoyl}amino)phenyl sulfamate inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004064molecular_functionarylesterase activity
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0018820molecular_functioncyanamide hydratase activity
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
B0004064molecular_functionarylesterase activity
B0004089molecular_functioncarbonate dehydratase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0018820molecular_functioncyanamide hydratase activity
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS94
AHIS96
AHIS119
AGZE306

site_idAC2
Number of Residues7
Detailsbinding site for residue ACT A 302
ChainResidue
BGZE303
BHOH421
APRO202
ATYR204
AGZE306
BALA132
BTYR204

site_idAC3
Number of Residues5
Detailsbinding site for residue ACT A 303
ChainResidue
AHIS103
AGLY104
ASER105
AASN245
AHOH427

site_idAC4
Number of Residues3
Detailsbinding site for residue GOL A 304
ChainResidue
AALA138
AASP139
AHOH485

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 305
ChainResidue
ATHR35
APHE260
AHOH425
AHOH433
BHOH430

site_idAC6
Number of Residues19
Detailsbinding site for residue GZE A 306
ChainResidue
AHIS67
APHE91
AGLN92
AHIS94
AHIS96
AHIS119
ALEU131
AALA135
ALEU141
ALEU198
ATHR199
AHIS200
APRO202
ATYR204
ATRP209
AZN301
AACT302
AHOH447
BGLU133

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119
BGZE303

site_idAC8
Number of Residues7
Detailsbinding site for residue GOL B 302
ChainResidue
BLYS149
BSER215
BILE216
BSER217
BHOH547
BHOH587
BHOH618

site_idAC9
Number of Residues18
Detailsbinding site for residue GZE B 303
ChainResidue
AALA132
ATYR204
AACT302
BHIS67
BGLN92
BHIS94
BHIS96
BHIS119
BLEU131
BALA135
BLEU198
BTHR199
BHIS200
BPRO202
BTYR204
BTRP209
BZN301
BHOH598

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdgvkYsaELHVA
ChainResidueDetails
ASER105-ALA121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS64
BHIS64

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: in variant Michigan-1 => ECO:0000269|PubMed:12009884
ChainResidueDetails
AHIS64
AHIS67
AHIS200
BHIS64
BHIS67
BHIS200

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362
ChainResidueDetails
AHIS94
AHIS96
AHIS119
BHIS94
BHIS96
BHIS119

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8057362
ChainResidueDetails
ATHR199
BTHR199

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:4207120, ECO:0000269|PubMed:4217196
ChainResidueDetails
AALA1
BALA1

218853

PDB entries from 2024-04-24

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