› 3iur

X-ray diffraction
2.05Å resolution

apPEP_D266Nx+H2H3 opened state

Released:
DOI: 10.2210/pdb3iur/pdb
PDB entry 3iur coloured by chain, front view.
PDB entry 3iur coloured by chain, side view.
PDB entry 3iur coloured by chain, top view.
Source organism: Aeromonas caviae
Primary publication:
Induced-fit mechanism for prolyl endopeptidase.
Li M, Chen C, Davies DR, Chiu TK
J Biol Chem 285 21487-95 (2010)
PMID: 20444688

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 trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163672 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
prolyl oligopeptidase Chain: A
Molecule details ›
Chain: A
Length: 693 amino acids
Theoretical weight: 77.03 KDa
Source organism: Aeromonas caviae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X6R4 (Residues: 1-690; Coverage: 100%)
Sequence domains:
Structure domains:
H2H3 helices from villin headpiece subdomain HP35 Chains: B, C
Molecule details ›
Chains: B, C
Length: 24 amino acids
Theoretical weight: 2.88 KDa
Source organism: Aeromonas caviae
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand GOL 3 x GOL
Ligand 15P 1 x 15P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 63.957Å b: 95.039Å c: 163.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.211
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

5 review citations

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

2 mentions without citation

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