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1AZM

DRUG-PROTEIN INTERACTIONS: STRUCTURE OF SULFONAMIDE DRUG COMPLEXED WITH HUMAN CARBONIC ANHYDRASE I

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 261
ChainResidue
AHIS94
AHIS96
AHIS119
AAZM262

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AZM A 262
ChainResidue
APHE91
AHIS94
AHIS96
AHIS119
ALEU198
ATHR199
AHIS200
ATRP209
AZN261
AHOH318
AHOH360

site_idCAT
Number of Residues24
DetailsCATALYTIC SITE
ChainResidue
ATYR7
ATHR199
AHIS200
APHE91
AALA121
ALEU131
AALA135
ALEU141
AVAL143
ALEU198
APRO201
AVAL62
APRO202
ATYR204
ASER206
AVAL207
ATRP209
AHIS64
ASER65
AHIS67
AASN69
AGLN92
AGLU106
AGLU117

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 Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ASER65

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: in variant Michigan-1 => ECO:0000269|PubMed:12009884
ChainResidueDetails
ASER65
AVAL68
APRO201

site_idSWS_FT_FI3
Number of Residues3
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
APHE95
ATRP97
AVAL120

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:8057362
ChainResidueDetails
AHIS200

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:4207120, ECO:0000269|PubMed:4217196
ChainResidueDetails
ASER2

218853

PDB entries from 2024-04-24

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