› 1e5t

X-ray diffraction
1.7Å resolution

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT

Released:
DOI: 10.2210/pdb1e5t/pdb
PDB entry 1e5t coloured by chain, front view.
PDB entry 1e5t coloured by chain, side view.
PDB entry 1e5t coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.
Fülöp V, Szeltner Z, Polgár L
EMBO Rep 1 277-81 (2000)
PMID: 11256612

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: 80.84 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 9 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 70.7Å b: 99.7Å c: 110.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.206
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Celiac disease: from pathogenesis to novel therapies.
Schuppan et al. (2009)
8 more

4 mentions without citation

Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.
Fülöp et al. (2000)
3 more