› 3b3c

X-ray diffraction
1.46Å resolution

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

Released:
DOI: 10.2210/pdb3b3c/pdb
PDB entry 3b3c coloured by chain, front view.
PDB entry 3b3c coloured by chain, side view.
PDB entry 3b3c coloured by chain, top view.
Source organism: Vibrio proteolyticus
Primary publication:
Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus.
Ataie NJ, Hoang QQ, Zahniser MP, Tu Y, Milne A, Petsko GA, Ringe D
Biochemistry 47 7673-83 (2008)
PMID: 18576673

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169609 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: Q01693 (Residues: 107-397; Coverage: 60%)
Sequence domains: Peptidase family M28
Structure domains: Zn peptidases

Ligands and Environments

5 bound ligands:
Ligand ZN 2 x ZN
Ligand K 1 x K
Ligand SCN 1 x SCN
Ligand NA 6 x NA
Ligand PLU 1 x PLU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P6122
Unit cell:
a: 108.189Å b: 108.189Å c: 97.206Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.197 0.226
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

Metallo-aminopeptidase inhibitors.
Mucha et al. (2010)
7 more

3 mentions without citation

Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus.
Ataie et al. (2008)
2 more