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2OFJ

Crystal structure of the E190A mutant of o-succinylbenzoate synthase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0009234biological_processmenaquinone biosynthetic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0043748molecular_functionO-succinylbenzoate synthase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0009234biological_processmenaquinone biosynthetic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0043748molecular_functionO-succinylbenzoate synthase activity
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0009234biological_processmenaquinone biosynthetic process
C0016829molecular_functionlyase activity
C0016836molecular_functionhydro-lyase activity
C0043748molecular_functionO-succinylbenzoate synthase activity
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0009234biological_processmenaquinone biosynthetic process
D0016829molecular_functionlyase activity
D0016836molecular_functionhydro-lyase activity
D0043748molecular_functionO-succinylbenzoate synthase activity
D0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10978150","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10978150","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10978150","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
ALYS133
ALYS235

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
BLYS133
BLYS235

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
CLYS133
CLYS235

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
DLYS133
DLYS235

site_idMCSA1
Number of Residues5
DetailsM-CSA 689
ChainResidueDetails
ALYS133proton acceptor, proton donor
AASP161metal ligand
AALA190metal ligand
AASP213metal ligand
ALYS235electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 689
ChainResidueDetails
BLYS133proton acceptor, proton donor
BASP161metal ligand
BALA190metal ligand
BASP213metal ligand
BLYS235electrostatic stabiliser

site_idMCSA3
Number of Residues5
DetailsM-CSA 689
ChainResidueDetails
CLYS133proton acceptor, proton donor
CASP161metal ligand
CALA190metal ligand
CASP213metal ligand
CLYS235electrostatic stabiliser

site_idMCSA4
Number of Residues5
DetailsM-CSA 689
ChainResidueDetails
DLYS133proton acceptor, proton donor
DASP161metal ligand
DALA190metal ligand
DASP213metal ligand
DLYS235electrostatic stabiliser

244693

PDB entries from 2025-11-12

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