› 2bws

X-ray diffraction
1.75Å resolution

Function and Biology Details

Reaction catalysed: 
Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147180 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xaa-Pro aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 440 amino acids
Theoretical weight: 49.69 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P15034 (Residues: 2-441; Coverage: 100%)
Gene names: JW2876, b2908, pepP
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MN 2 x MN
Ligand CL 1 x CL
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200H
Spacegroup: P6422
Unit cell:
a: 177.147Å b: 177.147Å c: 96.438Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.15 0.15 0.165
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Human prolidase and prolidase deficiency: an overview on the characterization of the enzyme involved in proline recycling and on the effects of its mutations.
Lupi et al. (2008)
3 more

1 mention without citation

Degradation of the microbial stress protectants and chemical chaperones ectoine and hydroxyectoine by a bacterial hydrolase-deacetylase complex.
Mais et al. (2020)