› 5b19

X-ray diffraction
1.85Å resolution

Picrophilus torridus aspartate racemase

Released:
DOI: 10.2210/pdb5b19/pdb
PDB entry 5b19 coloured by chain, front view.
PDB entry 5b19 coloured by chain, side view.
PDB entry 5b19 coloured by chain, top view.
Source organism: Picrophilus oshimae DSM 9789
Primary publication:
Structural and functional characterization of aspartate racemase from the acidothermophilic archaeon Picrophilus torridus.
Aihara T, Ito T, Yamanaka Y, Noguchi K, Odaka M, Sekine M, Homma H, Yohda M
Extremophiles 20 385-93 (2016)
PMID: 27094682

Function and Biology Details

Reaction catalysed: 
L-aspartate = D-aspartate
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-179841 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate racemase Chains: A, B
Molecule details ›
Chains: A, B
Length: 232 amino acids
Theoretical weight: 25.96 KDa
Source organism: Picrophilus oshimae DSM 9789
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6L2R8 (Residues: 1-232; Coverage: 100%)
Gene name: PTO0149
Sequence domains: Asp/Glu/Hydantoin racemase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P213
Unit cell:
a: 111.506Å b: 111.506Å c: 111.506Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.239 0.269
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Molecular cloning and enzymological characterization of pyridoxal 5'-phosphate independent aspartate racemase from hyperthermophilic archaeon Thermococcus litoralis DSM 5473.
Washio et al. (2016)
2 more

3 mentions without citation

Mechanisms of coronavirus cell entry mediated by the viral spike protein.
Belouzard et al. (2012)
2 more