X-ray diffraction
2.5Å resolution

Crystal structure of E.coli MenD, 2-succinyl-5-enolpyruvyl-6-hydroxy- 3-cyclohexadiene-1-carboxylate synthase - native protein


Function and Biology Details

Reaction catalysed:
Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO(2)
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 577 amino acids
Theoretical weight: 63.85 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
  • Canonical: P17109 (Residues: 1-556; Coverage: 100%)
Gene names: JW5374, b2264, menD
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand TPP 2 x TPP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P6522
Unit cell:
a: 93.425Å b: 93.425Å c: 465.172Å
α: 90° β: 90° γ: 120°
R R work R free
0.211 0.213 0.293
Expression system: Escherichia coli