› 1h2w

X-ray diffraction
1.39Å resolution

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN

Released:
DOI: 10.2210/pdb1h2w/pdb
PDB entry 1h2w coloured by chain, front view.
PDB entry 1h2w coloured by chain, side view.
PDB entry 1h2w coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site.
Szeltner Z, Rea D, Renner V, Fulop V, Polgar L
J Biol Chem 277 42613-22 (2002)
PMID: 12202494

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: 80.86 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 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P212121
Unit cell:
a: 71.6Å b: 100.1Å c: 111.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.23
Expression system: Escherichia coli

Quick links

Citations

14 citation in other articles

Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding.
Szeltner et al. (2004)
13 more

10 mentions without citation

Molecular, functional and structural properties of the prolyl oligopeptidase of Trypanosoma cruzi (POP Tc80), which is required for parasite entry into mammalian cells.
Bastos et al. (2005)
9 more