3mun

X-ray diffraction
2.1Å resolution

APPEP_PEPCLOSE closed state

Released:
Source organism: Aeromonas caviae
Entry author: Chiu TK

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-194950 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
prolyl oligopeptidase Chain: A
Molecule details ›
Chain: A
Length: 693 amino acids
Theoretical weight: 77.28 KDa
Source organism: Aeromonas caviae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X6R4 (Residues: 1-690; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3121
Unit cell:
a: 108.14Å b: 108.14Å c: 147.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.174 0.206
Expression system: Escherichia coli