› 2xdw

X-ray diffraction
1.35Å resolution

Inhibition of Prolyl Oligopeptidase with a Synthetic Unnatural Dipeptide

Released:
DOI: 10.2210/pdb2xdw/pdb
PDB entry 2xdw coloured by chain, front view.
PDB entry 2xdw coloured by chain, side view.
PDB entry 2xdw coloured by chain, top view.
Source organisms:
Primary publication:
Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide.
Racys DT, Rea D, Fülöp V, Wills M
Bioorg Med Chem 18 4775-82 (2010)
PMID: 20627594

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 analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150047 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Prolyl endopeptidase Chain: A
Molecule details ›
Chain: A
Length: 710 amino acids
Theoretical weight: 80.86 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P23687 (Residues: 1-710; Coverage: 100%)
Gene name: PREP
Sequence domains:
Structure domains:
SYNTHETIC PEPTIDE PHQ-PRO-YCP Chain: P
Molecule details ›
Chain: P
Length: 3 amino acids
Theoretical weight: 379 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand TAM 1 x TAM
Ligand GOL 9 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 70.82Å b: 99.51Å c: 110.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.164 0.186
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

Enzyme Tunnels and Gates As Relevant Targets in Drug Design.
Marques et al. (2017)
1 more

5 mentions without citation

Non-Canonical Amino Acids in Analyses of Protease Structure and Function.
Goettig et al. (2023)
4 more