› 3iuj

X-ray diffraction
1.8Å resolution

apPEP_WT2 opened state

Released:
DOI: 10.2210/pdb3iuj/pdb
PDB entry 3iuj coloured by chain, front view.
PDB entry 3iuj coloured by chain, side view.
PDB entry 3iuj coloured by chain, top view.
Source organism: Aeromonas caviae
Primary publication:
Induced-fit mechanism for prolyl endopeptidase.
Li M, Chen C, Davies DR, Chiu TK
J Biol Chem 285 21487-95 (2010)
PMID: 20444688

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194950 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
prolyl oligopeptidase Chain: A
Molecule details ›
Chain: A
Length: 693 amino acids
Theoretical weight: 77.4 KDa
Source organism: Aeromonas caviae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X6R4 (Residues: 1-690; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 62.64Å b: 85.131Å c: 148.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.218
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Low molecular weight inhibitors of Prolyl Oligopeptidase: a review of compounds patented from 2003 to 2010.
López et al. (2011)
5 more

2 mentions without citation

Induced-fit mechanism for prolyl endopeptidase.
Li et al. (2010)
1 more