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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3JS3

Crystal structure of type I 3-dehydroquinate dehydratase (aroD) from Clostridium difficile with covalent reaction intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003855molecular_function3-dehydroquinate dehydratase activity
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0016829molecular_functionlyase activity
A0046279biological_process3,4-dihydroxybenzoate biosynthetic process
B0003855molecular_function3-dehydroquinate dehydratase activity
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0009423biological_processchorismate biosynthetic process
B0016829molecular_functionlyase activity
B0046279biological_process3,4-dihydroxybenzoate biosynthetic process
C0003855molecular_function3-dehydroquinate dehydratase activity
C0008652biological_processamino acid biosynthetic process
C0009073biological_processaromatic amino acid family biosynthetic process
C0009423biological_processchorismate biosynthetic process
C0016829molecular_functionlyase activity
C0046279biological_process3,4-dihydroxybenzoate biosynthetic process
D0003855molecular_function3-dehydroquinate dehydratase activity
D0008652biological_processamino acid biosynthetic process
D0009073biological_processaromatic amino acid family biosynthetic process
D0009423biological_processchorismate biosynthetic process
D0016829molecular_functionlyase activity
D0046279biological_process3,4-dihydroxybenzoate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DHS A 301
ChainResidue
AGLU47
AGLN237
AHOH282
AHOH304
AARG49
AARG83
ALYS171
AMET204
AARG214
APHE226
ASER233
AALA234
site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DHS B 301
ChainResidue
BGLU47
BARG49
BARG83
BHIS144
BLYS171
BMET204
BARG214
BPHE226
BSER233
BALA234
BGLN237
BHOH321
BHOH322
site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE DHS C 301
ChainResidue
CGLU47
CARG49
CARG83
CLYS171
CMET204
CARG214
CPHE226
CSER233
CALA234
CGLN237
CHOH278
site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DHS D 301
ChainResidue
DGLU47
DARG49
DARG83
DHIS144
DLYS171
DMET204
DARG214
DPHE226
DSER233
DALA234
DGLN237
DHOH320
Functional Information from PROSITE/UniProt
site_idPS01028
Number of Residues31
DetailsDEHYDROQUINASE_I Dehydroquinase class I active site. DVELfmgdevidevvnfahkkevkVIiSNHD
ChainResidueDetails
AASP115-ASP145
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"1.95 Angstrom crystal structure of type I 3-dehydroquinate dehydratase (aroD) from Clostridium difficile with covalent modified comenic acid.","authoringGroup":["Center for Structural Genomics of Infectious Diseases (CSGID)"],"authors":["Minasov G.","Light S.H.","Shuvalova L.","Duban M.E.","Dubrovska I.","Winsor J.","Papazisi L.","Anderson W.F."]}}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21087925","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"1.95 Angstrom crystal structure of type I 3-dehydroquinate dehydratase (aroD) from Clostridium difficile with covalent modified comenic acid.","authoringGroup":["Center for Structural Genomics of Infectious Diseases (CSGID)"],"authors":["Minasov G.","Light S.H.","Shuvalova L.","Duban M.E.","Dubrovska I.","Winsor J.","Papazisi L.","Anderson W.F."]}}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21087925","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21087925","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"1.95 Angstrom crystal structure of type I 3-dehydroquinate dehydratase (aroD) from Clostridium difficile with covalent modified comenic acid.","authoringGroup":["Center for Structural Genomics of Infectious Diseases (CSGID)"],"authors":["Minasov G.","Light S.H.","Shuvalova L.","Duban M.E.","Dubrovska I.","Winsor J.","Papazisi L.","Anderson W.F."]}}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qfe
ChainResidueDetails
AGLU87
AHIS144
ALYS171
site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qfe
ChainResidueDetails
BGLU87
BHIS144
BLYS171
site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qfe
ChainResidueDetails
CGLU87
CHIS144
CLYS171
site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qfe
ChainResidueDetails
DGLU87
DHIS144
DLYS171

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