X-ray diffraction
1.9Å resolution

Crystal structure of Escherichia coli glutamate racemase in complex with L- Glutamate and activator UDP-MurNAc-ala


Function and Biology Details

Reaction catalysed:
L-glutamate = D-glutamate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Glutamate racemase Chain: A
Molecule details ›
Chain: A
Length: 285 amino acids
Theoretical weight: 31.03 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P22634 (Residues: 1-285; Coverage: 100%)
Gene names: JW5550, b3967, dga, glr, murI, yijA
Sequence domains: Asp/Glu/Hydantoin racemase
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2221
Unit cell:
a: 83.05Å b: 112.82Å c: 74.12Å
α: 90° β: 90° γ: 90°
R R work R free
0.218 0.218 0.244
Expression system: Escherichia coli