› 1h2y

X-ray diffraction
1.78Å resolution

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL

Released:
DOI: 10.2210/pdb1h2y/pdb
PDB entry 1h2y coloured by chain, front view.
PDB entry 1h2y coloured by chain, side view.
PDB entry 1h2y 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: 80.85 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

2 bound ligands:
Ligand ZPR 1 x ZPR
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P212121
Unit cell:
a: 70.8Å b: 99.6Å c: 110.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 0.194
Expression system: Escherichia coli

Quick links

Citations

17 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)
16 more

2 mentions without citation

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