PDBe 1a16

X-ray diffraction
2.3Å resolution

AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU

Released:
Source organism: Escherichia coli
Primary publication:
Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli.
Proc. Natl. Acad. Sci. U.S.A. 95 3472-7 (1998)
PMID: 9520390

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:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xaa-Pro aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 440 amino acids
Theoretical weight: 49.74 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P15034 (Residues: 2-441; Coverage: 100%)
Gene names: JW2876, b2908, pepP
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P6422
Unit cell:
a: 177.3Å b: 177.3Å c: 96.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.184 0.226