› 1vz2

X-ray diffraction
2.2Å resolution

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANT

Released:
DOI: 10.2210/pdb1vz2/pdb
PDB entry 1vz2 coloured by chain, front view.
PDB entry 1vz2 coloured by chain, side view.
PDB entry 1vz2 coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding.
Szeltner Z, Rea D, Juhász T, Renner V, Fülöp V, Polgár L
J Mol Biol 340 627-37 (2004)
PMID: 15210359

Function and Biology Details

Reaction catalysed: 
Hydrolysis of --Pro-|- and to a lesser extent --Ala-|- in oligopeptides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150042 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prolyl endopeptidase Chain: A
Molecule details ›
Chain: A
Length: 710 amino acids
Theoretical weight: 80.81 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P23687 (Residues: 1-710; Coverage: 100%)
Gene name: PREP
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P212121
Unit cell:
a: 70.9Å b: 99.6Å c: 110Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.163 0.208
Expression system: Escherichia coli

Quick links

Citations

5 review citations

On the role of prolyl oligopeptidase in health and disease.
García-Horsman et al. (2007)
4 more

2 mentions without citation

Towards the prediction of protein interaction partners using physical docking.
Wass et al. (2011)
1 more