PDBe 1amp

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF AEROMONAS PROTEOLYTICA AMINOPEPTIDASE: A PROTOTYPICAL MEMBER OF THE CO-CATALYTIC ZINC ENZYME FAMILY

Released:

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacterial leucyl aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 291 amino acids
Theoretical weight: 31.43 KDa
Source organism: Vibrio proteolyticus
Expression system: Not provided
UniProt:
  • Canonical: Q01693 (Residues: 107-397; Coverage: 60%)
Sequence domains: Peptidase family M28
Structure domains: Zn peptidases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6122
Unit cell:
a: 111Å b: 111Å c: 92.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.161 0.161 not available
Expression system: Not provided