› 1uoq

X-ray diffraction
2.1Å resolution

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND GLU-PHE-SER-PRO

Released:
DOI: 10.2210/pdb1uoq/pdb
PDB entry 1uoq coloured by chain, front view.
PDB entry 1uoq coloured by chain, side view.
PDB entry 1uoq coloured by chain, top view.
Source organisms:
Primary publication:
Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding.
Szeltner Z, Rea D, Renner V, Juliano L, Fülop V, Polgár L
J Biol Chem 278 48786-93 (2003)
PMID: 14514675

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150046 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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:
PEPTIDE LIGAND GLU-PHE-SER-PRO Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 478 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P212121
Unit cell:
a: 70.3Å b: 99.1Å c: 109.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.147 0.205
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

Low molecular weight inhibitors of Prolyl Oligopeptidase: a review of compounds patented from 2003 to 2010.
López et al. (2011)
17 other articles

1 mention without citation

Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
Soisson et al. (2010)