› 2ohv

X-ray diffraction
2.5Å resolution

Structural Basis for Glutamate Racemase Inhibition

Released:
DOI: 10.2210/pdb2ohv/pdb
PDB entry 2ohv coloured by chain, front view.
PDB entry 2ohv coloured by chain, side view.
PDB entry 2ohv coloured by chain, top view.
Source organism: Streptococcus pyogenes M1 GAS
Primary publication:
Structural basis for glutamate racemase inhibition.
Kim KH, Bong YJ, Park JK, Shin KJ, Hwang KY, Kim EE
J Mol Biol 372 434-43 (2007)
PMID: 17658548

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-189453 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate racemase Chain: A
Molecule details ›
Chain: A
Length: 264 amino acids
Theoretical weight: 29.05 KDa
Source organism: Streptococcus pyogenes M1 GAS
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9A1B7 (Residues: 1-264; Coverage: 100%)
Gene names: M5005_Spy0303, SPy_0361, glr, murI
Sequence domains: Asp/Glu/Hydantoin racemase
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand NHL 1 x NHL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P3221
Unit cell:
a: 79.745Å b: 79.745Å c: 95.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.226 0.237
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Cytoplasmic steps of peptidoglycan biosynthesis.
Barreteau et al. (2008)
2 more

1 mention 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)