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2OZT

Crystal structure of O-succinylbenzoate synthase from Thermosynechococcus elongatus BP-1

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 Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 601
ChainResidue
ATHR132
ALYS161
AARG163
AGLU191
ACYS291
AHIS292
AALA293
AHOH800
AHOH1061

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 602
ChainResidue
AASP171
AARG172
AGLN201
AHOH719
AHOH1031

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 701
ChainResidue
AASP165
AASN167
AGLU194
AGLN195
AASP219
AGLU220

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

245011

PDB entries from 2025-11-19

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