› 1qfm

X-ray diffraction
1.4Å resolution

PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE

Released:
DOI: 10.2210/pdb1qfm/pdb
PDB entry 1qfm coloured by chain, front view.
PDB entry 1qfm coloured by chain, side view.
PDB entry 1qfm 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: 80.98 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P23687 (Residues: 1-710; Coverage: 100%)
Gene name: PREP
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SGL 2 x SGL
Ligand SGM 2 x SGM
Ligand GOL 4 x GOL
2 modified residues:
Ligand CSX 3 x CSX
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P212121
Unit cell:
a: 70.7Å b: 99.6Å c: 110.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.206

Quick links

Citations

34 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)
33 more

11 mentions without citation

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