› 1sjc

X-ray diffraction
2.1Å resolution

x-ray structure of o-succinylbenzoate synthase complexed with N-succinyl methionine

Released:
DOI: 10.2210/pdb1sjc/pdb
PDB entry 1sjc coloured by chain, front view.
PDB entry 1sjc coloured by chain, side view.
PDB entry 1sjc coloured by chain, top view.
Source organism: Amycolatopsis sp.
Primary publication:
Evolution of enzymatic activity in the enolase superfamily: structural studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis.
Thoden JB, Taylor Ringia EA, Garrett JB, Gerlt JA, Holden HM, Rayment I
Biochemistry 43 5716-27 (2004)
PMID: 15134446

Function and Biology Details

Reaction catalysed: 
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175018 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-succinylamino acid racemase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 368 amino acids
Theoretical weight: 39.45 KDa
Source organism: Amycolatopsis sp.
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q44244 (Residues: 1-368; Coverage: 100%)
Gene name: Aaar
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand SMG 4 x SMG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: R32
Unit cell:
a: 215.7Å b: 215.7Å c: 259Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.208 0.274
Expression system: Escherichia coli BL21

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Citations

6 review citations

Enzyme promiscuity: mechanism and applications.
Hult et al. (2007)
5 more

3 mentions without citation

Characterization of iron dinitrosyl species formed in the reaction of nitric oxide with a biological Rieske center.
Tinberg et al. (2010)
2 more