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3H7V

CRYSTAL STRUCTURE OF O-SUCCINYLBENZOATE SYNTHASE FROM THERMOSYNECHOCOCCUS ELONGATUS BP-1 complexed with MG in the active site

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0009234biological_processmenaquinone biosynthetic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0042372biological_processphylloquinone biosynthetic process
A0043748molecular_functionO-succinylbenzoate synthase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 331
ChainResidue
AASP165
AGLU194
AASP219
AHOH379
AHOH382
AHOH425

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

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00470","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24872444","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3H7V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
ALYS136
ALYS243

249697

PDB entries from 2026-02-25

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