PDBe 1jfl

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE DETERMINATION OF ASPARTATE RACEMASE FROM AN ARCHAEA

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate racemase Chains: A, B
Molecule details ›
Chains: A, B
Length: 228 amino acids
Theoretical weight: 25.19 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O58403 (Residues: 1-228; Coverage: 100%)
Gene name: PH0670
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: PHOTON FACTORY BEAMLINE BL-6A, SPRING-8 BEAMLINE BL44B2
Spacegroup: P21
Unit cell:
a: 65.481Å b: 58.685Å c: 67.035Å
α: 90° β: 109.62° γ: 90°
R-values:
R R work R free
0.194 0.194 0.222
Expression system: Escherichia coli