› 1lry

X-ray diffraction
2.6Å resolution

Crystal Structure of P. aeruginosa Peptide Deformylase Complexed with Antibiotic Actinonin

Released:
DOI: 10.2210/pdb1lry/pdb
PDB entry 1lry coloured by chain, front view.
PDB entry 1lry coloured by chain, side view.
PDB entry 1lry coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents.
Guilloteau JP, Mathieu M, Giglione C, Blanc V, Dupuy A, Chevrier M, Gil P, Famechon A, Meinnel T, Mikol V
J Mol Biol 320 951-62 (2002)
PMID: 12126617

Function and Biology Details

Reaction catalysed: 
Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide
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-191502 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide deformylase Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 19.26 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9I7A8 (Residues: 2-168; Coverage: 99%)
Gene names: PA0019, def
Sequence domains: Polypeptide deformylase
Structure domains: Peptide deformylase

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand BB2 1 x BB2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS
Spacegroup: P212121
Unit cell:
a: 50.43Å b: 60.13Å c: 73.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 not available
Expression system: Escherichia coli

Quick links

Citations

12 review citations

The design of inhibitors for medicinally relevant metalloproteins.
Jacobsen et al. (2007)
11 more

6 mentions without citation

Copaifera of the Neotropics: A Review of the Phytochemistry and Pharmacology.
da Trindade et al. (2018)
5 more