› 1fhu

X-ray diffraction
1.65Å resolution

CRYSTAL STRUCTURE ANALYSIS OF O-SUCCINYLBENZOATE SYNTHASE FROM E. COLI

Released:
DOI: 10.2210/pdb1fhu/pdb
PDB entry 1fhu coloured by chain, front view.
PDB entry 1fhu coloured by chain, side view.
PDB entry 1fhu coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate.
Thompson TB, Garrett JB, Taylor EA, Meganathan R, Gerlt JA, Rayment I
Biochemistry 39 10662-76 (2000)
PMID: 10978150

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151368 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
o-succinylbenzoate synthase Chain: A
Molecule details ›
Chain: A
Length: 320 amino acids
Theoretical weight: 35.51 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P29208 (Residues: 1-320; Coverage: 100%)
Gene names: JW2256, b2261, menC
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 56.1Å b: 70Å c: 80.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.265
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
4 more

3 mentions without citation

Catalytic site identification--a web server to identify catalytic site structural matches throughout PDB.
Kirshner et al. (2013)
2 more