› 1cp6

X-ray diffraction
1.9Å resolution

1-BUTANEBORONIC ACID BINDING TO AEROMONAS PROTEOLYTICA AMINOPEPTIDASE

Released:
DOI: 10.2210/pdb1cp6/pdb
PDB entry 1cp6 coloured by chain, front view.
PDB entry 1cp6 coloured by chain, side view.
PDB entry 1cp6 coloured by chain, top view.
Source organism: Vibrio proteolyticus
Primary publication:
1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development.
De Paola CC, Bennett B, Holz RC, Ringe D, Petsko GA
Biochemistry 38 9048-53 (1999)
PMID: 10413478

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:
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: 31.43 KDa
Source organism: Vibrio proteolyticus
UniProt:
  • Canonical: Q01693 (Residues: 107-397; Coverage: 60%)
Sequence domains: Peptidase family M28
Structure domains: Zn peptidases

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand BUB 1 x BUB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6122
Unit cell:
a: 109.2Å b: 109.2Å c: 97.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.193 0.229

Quick links

Citations

1 review citation

Structures and mechanisms of Nudix hydrolases.
Mildvan et al. (2005)
18 other articles

1 mention without citation

Experimental evidence for a metallohydrolase mechanism in which the nucleophile is not delivered by a metal ion: EPR spectrokinetic and structural studies of aminopeptidase from Vibrio proteolyticus.
Kumar et al. (2007)