› 1n51

X-ray diffraction
2.3Å resolution

Aminopeptidase P in complex with the inhibitor apstatin

Released:
DOI: 10.2210/pdb1n51/pdb
PDB entry 1n51 coloured by chain, front view.
PDB entry 1n51 coloured by chain, side view.
PDB entry 1n51 coloured by chain, top view.
Source organisms:
Primary publication:
Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin.
Graham SC, Maher MJ, Simmons WH, Freeman HC, Guss JM
Acta Crystallogr D Biol Crystallogr 60 1770-9 (2004)
PMID: 15388923

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

Assemblies composition:
hetero octamer
hetero tetramer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-147179 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Xaa-Pro aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 440 amino acids
Theoretical weight: 49.74 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:
apstatin Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 459 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand MN 3 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I4122
Unit cell:
a: 139.319Å b: 139.319Å c: 231.005Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.204
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

11 citation in other articles

Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability.
Vögtle et al. (2009)
10 more

1 mention without citation

A Molecular Analysis of the Aminopeptidase P-Related Domain of PID-5 from Caenorhabditis elegans.
Lloyd et al. (2023)