› 1jfl

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE DETERMINATION OF ASPARTATE RACEMASE FROM AN ARCHAEA

Released:
DOI: 10.2210/pdb1jfl/pdb
PDB entry 1jfl coloured by chain, front view.
PDB entry 1jfl coloured by chain, side view.
PDB entry 1jfl coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization.
Liu L, Iwata K, Kita A, Kawarabayasi Y, Yohda M, Miki K
J Mol Biol 319 479-89 (2002)
PMID: 12051922

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129718 (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

Quick links

Citations

4 review citations

Bacterial synthesis of D-amino acids.
Radkov et al. (2014)
3 more

9 mentions without citation

Structural space of protein-protein interfaces is degenerate, close to complete, and highly connected.
Gao et al. (2010)
8 more