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3CAW

Crystal structure of o-succinylbenzoate synthase from Bdellovibrio bacteriovorus liganded with Mg

Functional Information from GO Data
ChainGOidnamespacecontents
A0009234biological_processmenaquinone biosynthetic process
A0016829molecular_functionlyase activity
A0042372biological_processphylloquinone biosynthetic process
A0043748molecular_functionO-succinylbenzoate synthase activity
A0046872molecular_functionmetal ion binding
B0009234biological_processmenaquinone biosynthetic process
B0016829molecular_functionlyase activity
B0042372biological_processphylloquinone biosynthetic process
B0043748molecular_functionO-succinylbenzoate synthase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP155
AGLU184
AASP206

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASP155
BGLU184
BASP206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P29208","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P29208","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24872444","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CAW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
ALYS228
ALYS130

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
BLYS228
BLYS130

243531

PDB entries from 2025-10-22

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