› 2bwt

X-ray diffraction
2.9Å 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: 49.7 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

4 bound ligands:
Ligand MN 1 x MN
Ligand MG 1 x MG
Ligand FLC 1 x FLC
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: I4122
Unit cell:
a: 137.588Å b: 137.588Å c: 231.948Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.202
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

Metagenomics: Retrospect and Prospects in High Throughput Age.
Kumar et al. (2015)