› 1amp

X-ray diffraction
1.8Å resolution

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

Released:
DOI: 10.2210/pdb1amp/pdb
PDB entry 1amp coloured by chain, front view.
PDB entry 1amp coloured by chain, side view.
PDB entry 1amp coloured by chain, top view.
Source organism: Vibrio proteolyticus
Primary publication:
Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family.
Chevrier B, Schalk C, D'Orchymont H, Rondeau JM, Moras D, Tarnus C
Structure 2 283-91 (1994)
PMID: 8087555

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169610 (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:
Ligand ZN 2 x ZN
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

Quick links

Citations

7 review citations

How far divergent evolution goes in proteins.
Murzin AG. (1998)
6 more

20 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
19 more