› 1a16

X-ray diffraction
2.3Å resolution

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

Released:
DOI: 10.2210/pdb1a16/pdb
PDB entry 1a16 coloured by chain, front view.
PDB entry 1a16 coloured by chain, side view.
PDB entry 1a16 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli.
Wilce MC, Bond CS, Dixon NE, Freeman HC, Guss JM, Lilley PE, Wilce JA
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:
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: 49.74 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:
Ligand PRO 1 x PRO
Ligand LEU 1 x LEU
Ligand MN 2 x MN
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

Quick links

Citations

10 review citations

Creatine and creatinine metabolism.
Wyss et al. (2000)
9 more

5 mentions without citation

Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes.
Yang et al. (2005)
4 more