› 1wl9

X-ray diffraction
1.9Å resolution

Structure of aminopeptidase P from E. coli

Released:
DOI: 10.2210/pdb1wl9/pdb
PDB entry 1wl9 coloured by chain, front view.
PDB entry 1wl9 coloured by chain, side view.
PDB entry 1wl9 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural and functional implications of metal ion selection in aminopeptidase P, a metalloprotease with a dinuclear metal center.
Graham SC, Bond CS, Freeman HC, Guss JM
Biochemistry 44 13820-36 (2005)
PMID: 16229471

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: 49.76 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 RU200
Spacegroup: P6422
Unit cell:
a: 177.42Å b: 177.42Å c: 96.42Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.152 0.152 0.17
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Metallostasis and amyloid β-degrading enzymes.
Grasso et al. (2012)
2 more

3 mentions without citation

Structure of the human aminopeptidase XPNPEP3 and comparison of its in vitro activity with Icp55 orthologs: Insights into diverse cellular processes.
Singh et al. (2017)
2 more