X-ray diffraction
2Å resolution

X-ray crystal structure of bestatin bound to AAP


Function and Biology Details

Reaction catalysed:
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Bacterial leucyl aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 299 amino acids
Theoretical weight: 32.24 KDa
Source organism: Vibrio proteolyticus
  • Canonical: Q01693 (Residues: 107-405; Coverage: 62%)
Sequence domains: Peptidase family M28
Structure domains: Zn peptidases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6122
Unit cell:
a: 107.8Å b: 107.8Å c: 102.6Å
α: 90° β: 90° γ: 120°
R R work R free
0.195 0.195 0.245