› 3eq7

X-ray diffraction
2.89Å resolution

Prolyl oligopeptidase complexed with R-Pro-(decarboxy-Pro)-Type inhibitors

Released:
DOI: 10.2210/pdb3eq7/pdb
PDB entry 3eq7 coloured by chain, front view.
PDB entry 3eq7 coloured by chain, side view.
PDB entry 3eq7 coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Prolyl oligopeptidase inhibition by N-acyl-pro-pyrrolidine-type molecules.
Kánai K, Arányi P, Böcskei Z, Ferenczy G, Harmat V, Simon K, Bátori S, Náray-Szabo G, Hermecz I
J Med Chem 51 7514-22 (2008)
PMID: 19006380

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-150042 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prolyl endopeptidase Chain: A
Molecule details ›
Chain: A
Length: 710 amino acids
Theoretical weight: 80.86 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P23687 (Residues: 1-710; Coverage: 100%)
Gene name: PREP
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand X99 1 x X99
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 72.44Å b: 101.44Å c: 112.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.257

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Citations

1 review citation

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