PDBe 1b73

X-ray diffraction
2.3Å resolution

GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS

Released:
Source organism: Aquifex pyrophilus
Primary publication:
Structure and mechanism of glutamate racemase from Aquifex pyrophilus.
Nat. Struct. Biol. 6 422-6 (1999)
PMID: 10331867

Function and Biology Details

Reaction catalysed:
L-glutamate = D-glutamate. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate racemase Chain: A
Molecule details ›
Chain: A
Length: 254 amino acids
Theoretical weight: 27.98 KDa
Source organism: Aquifex pyrophilus
UniProt:
  • Canonical: P56868 (Residues: 1-254; Coverage: 100%)
Gene name: murI
Sequence domains: Asp/Glu/Hydantoin racemase
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P6522
Unit cell:
a: 72.17Å b: 72.17Å c: 184.99Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.229 0.284