› 3ddu

X-ray diffraction
1.56Å resolution

Prolyl Oligopeptidase with GSK552

Released:
DOI: 10.2210/pdb3ddu/pdb
PDB entry 3ddu coloured by chain, front view.
PDB entry 3ddu coloured by chain, side view.
PDB entry 3ddu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of prolyl oligopeptidase (POP).
Haffner CD, Diaz CJ, Miller AB, Reid RA, Madauss KP, Hassell A, Hanlon MH, Porter DJ, Becherer JD, Carter LH
Bioorg Med Chem Lett 18 4360-3 (2008)
PMID: 18606544

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-155709 (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:
Ligand ACT 5 x ACT
Ligand 552 1 x 552
Ligand GOL 1 x GOL
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

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Citations

2 review citations

Parasite prolyl oligopeptidases and the challenge of designing chemotherapeuticals for Chagas disease, leishmaniasis and African trypanosomiasis.
Bastos et al. (2013)
1 more

15 mentions without citation

Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications.
Baharin et al. (2022)
14 more