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4WUP

Crystal structure of human carbonic anhydrase isozyme I with 4-[(2-Hydroxyethyl)thio]benzenesulfonamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004064molecular_functionarylesterase activity
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0009750biological_processresponse to fructose
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
B0008270molecular_functionzinc ion binding
B0009750biological_processresponse to fructose
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
A3UF302

site_idAC2
Number of Residues10
Detailsbinding site for residue 3UF A 302
ChainResidue
ALEU198
ATHR199
AHIS200
ATRP209
AZN301
AHIS94
AHIS96
AHIS119
AALA135
AVAL143

site_idAC3
Number of Residues2
Detailsbinding site for residue ACT A 303
ChainResidue
ATYR204
BTYR204

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119
B3UF302

site_idAC5
Number of Residues9
Detailsbinding site for residue 3UF B 302
ChainResidue
BHIS94
BHIS96
BHIS119
BVAL143
BLEU198
BTHR199
BHIS200
BTRP209
BZN301

site_idAC6
Number of Residues3
Detailsbinding site for residue PEG B 303
ChainResidue
BLYS170
BGLY171
BHOH478

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 Residues40
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"description":"in variant Michigan-1","evidences":[{"source":"PubMed","id":"12009884","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12009884","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16506782","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16870440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17314045","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17407288","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6430186","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7932756","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"804171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8057362","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8057362","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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