3rva

X-ray diffraction
1.8Å resolution

Crystal structure of organophosphorus acid anhydrolase from Alteromonas macleodii

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xaa-Pro dipeptidase Chain: A
Molecule details ›
Chain: A
Length: 451 amino acids
Theoretical weight: 51.52 KDa
Source organism: Alteromonas macleodii
Expression system: Escherichia coli
UniProt:
  • Canonical: F8UVJ4 (Residues: 1-443; Coverage: 100%)
Gene names: BFV94_0545, TE101_02590, pepQ
Sequence domains: Metallopeptidase family M24
Structure domains:

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2
Unit cell:
a: 133.77Å b: 49.19Å c: 97.34Å
α: 90° β: 125.03° γ: 90°
R-values:
R R work R free
0.156 0.156 not available
Expression system: Escherichia coli