› 2jfx

X-ray diffraction
2.3Å resolution

Crystal structure of Helicobacter pylori glutamate racemase in complex with D-Glutamate

Released:
DOI: 10.2210/pdb2jfx/pdb
PDB 2jfx coloured by chain and viewed from the front.
PDB 2jfx coloured by chain and viewed from the side.
PDB 2jfx coloured by chain and viewed from the top.
Source organism: Helicobacter pylori
Primary publication:
Exploitation of structural and regulatory diversity in glutamate racemases.
Lundqvist T, Fisher SL, Kern G, Folmer RH, Xue Y, Newton DT, Keating TA, Alm RA, de Jonge BL
Nature 447 817-22 (2007)
PMID: 17568739

Function and Biology Details

Reaction catalysed: 
L-glutamate = D-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate racemase Chains: A, B
Molecule details ›
Chains: A, B
Length: 255 amino acids
Theoretical weight: 28.53 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZLT0 (Residues: 1-255; Coverage: 100%)
Gene names: glr, jhp_0496, murI
Sequence domains: Asp/Glu/Hydantoin racemase
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand DGL 2 x DGL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 62.18Å b: 81.07Å c: 113.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.281
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition.
Lloyd et al. (2021)
8 more

4 mentions without citation

Flooding enzymes: quantifying the contributions of interstitial water and cavity shape to ligand binding using extended linear response free energy calculations.
Whalen et al. (2013)
3 more