X-ray diffraction
1.18Å resolution

Crystal structure of the M180A mutant of the aminopeptidase from Vibrio proteolyticus in complex with leucine


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: 291 amino acids
Theoretical weight: 31.37 KDa
Source organism: Vibrio proteolyticus
Expression system: Escherichia coli BL21
  • Canonical: Q01693 (Residues: 107-397; Coverage: 60%)
Sequence domains: Peptidase family M28
Structure domains: Zn peptidases

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P6122
Unit cell:
a: 109.485Å b: 109.485Å c: 91.022Å
α: 90° β: 90° γ: 120°
R R work R free
0.168 0.166 0.196
Expression system: Escherichia coli BL21