PDBe 3ddu

X-ray diffraction
1.56Å resolution

Prolyl Oligopeptidase with GSK552

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prolyl endopeptidase Chain: A
Molecule details ›
Chain: A
Length: 709 amino acids
Theoretical weight: 80.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48147 (Residues: 2-710; Coverage: 100%)
Gene names: PEP, PREP
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 71.221Å b: 99.883Å c: 111.853Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.147 0.172
Expression system: Escherichia coli