› 1qfs

X-ray diffraction
2Å resolution

PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL

Released:
DOI: 10.2210/pdb1qfs/pdb
PDB entry 1qfs coloured by chain, front view.
PDB entry 1qfs coloured by chain, side view.
PDB entry 1qfs coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis.
Fülöp V, Böcskei Z, Polgár L
Cell 94 161-70 (1998)
PMID: 9695945

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
UniProt:
  • Canonical: P23687 (Residues: 1-710; Coverage: 100%)
Gene name: PREP
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 70.9Å b: 99.8Å c: 110.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.243

Quick links

Citations

35 review citations

Dipeptidyl-peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV.
Lambeir et al. (2003)
34 more

12 mentions without citation

The two-step biosynthesis of cyclic peptides from linear precursors in a member of the plant family Caryophyllaceae involves cyclization by a serine protease-like enzyme.
Barber et al. (2013)
11 more