› 3rva

X-ray diffraction
1.8Å resolution

Crystal structure of organophosphorus acid anhydrolase from Alteromonas macleodii

Released:
DOI: 10.2210/pdb3rva/pdb
PDB entry 3rva coloured by chain, front view.
PDB entry 3rva coloured by chain, side view.
PDB entry 3rva coloured by chain, top view.
Source organism: Alteromonas macleodii
Primary publication:
Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases.
Štěpánková A, Dušková J, Skálová T, Hašek J, Koval' T, Østergaard LH, Dohnálek J
Acta Crystallogr Sect F Struct Biol Cryst Commun 69 346-54 (2013)
PMID: 23545636

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123734 (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, pepQ
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MN 2 x MN
Ligand PO4 1 x PO4
Ligand NI 1 x NI
1 modified residue:
Ligand CSO 1 x CSO

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

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Citations

1 review citation

Current and emerging strategies for organophosphate decontamination: special focus on hyperstable enzymes.
Jacquet et al. (2016)
3 other articles

2 mentions without citation

Structural basis of substrate selectivity of E. coli prolidase.
Weaver et al. (2014)
1 more