4an0

X-ray diffraction
2.2Å resolution

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A COVALENTLY BOUND INHIBITOR IC-3

Released:
Source organism: Sus scrofa
Entry authors: Kaszuba K, Rog T, Danne R, Canning P, Fulop V, Juhasz T, Szeltner Z, St-Pierre JF, Garcia-Horsman A, Mannisto PT, Karttunen M, Hokkanen J, Bunker A

Function and Biology Details

Reaction catalysed:
Hydrolysis of --Pro-|- and to a lesser extent --Ala-|- in oligopeptides.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM16
Spacegroup: P212121
Unit cell:
a: 71.3Å b: 99.9Å c: 111.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.222
Expression system: Escherichia coli