› 1sja

X-ray diffraction
2.3Å resolution

X-ray structure of o-Succinylbenzoate Synthase complexed with N-acetylmethionine

Released:
DOI: 10.2210/pdb1sja/pdb
PDB entry 1sja coloured by chain, front view.
PDB entry 1sja coloured by chain, side view.
PDB entry 1sja 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 AME 4 x AME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: R32
Unit cell:
a: 215.3Å b: 215.3Å c: 259.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.211 0.28
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

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

1 mention without citation

An approach to functionally relevant clustering of the protein universe: Active site profile-based clustering of protein structures and sequences.
Knutson et al. (2017)