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1CZM

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
AAAS262

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 264
ChainResidue
ALEU189
AHG266
AHG267
AHOH456
AHOH472

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 265
ChainResidue
ASER182
ALEU185
APRO186
AHOH270

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG A 266
ChainResidue
ACYS212
AHG264
AHG267
AHOH456
AHOH466
AHOH472

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HG A 267
ChainResidue
ASER188
AASP190
ACYS212
AHG264
AHG266
AHOH456
AHOH466
AHOH472

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 269
ChainResidue
AVAL146
ALEU147
ACYS212
AGLU214

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE AAS A 262
ChainResidue
AHIS94
AHIS96
AHIS119
ALEU198
ATHR199
AHIS200
AZN261

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR199
AHIS64

225946

PDB entries from 2024-10-09

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