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2OPJ

Crystal structure of O-succinylbenzoate synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0009063biological_processamino acid catabolic process
A0009234biological_processmenaquinone biosynthetic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0043748molecular_functionO-succinylbenzoate synthase activity
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00909
Number of Residues32
DetailsMR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. VriDvNgawdvdtAvrmirlLdrfeleyVEQP
ChainResidueDetails
AVAL127-PRO158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24060347","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QVH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24060347","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QVH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
AALA101
ALYS203

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
ALYS99
ALYS203

246704

PDB entries from 2025-12-24

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