› 1lqw

X-ray diffraction
1.87Å resolution

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-159509 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide deformylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 20.59 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P68826 (Residues: 1-183; Coverage: 100%)
Gene names: def, def1, pdf1
Sequence domains: Polypeptide deformylase
Structure domains: Peptide deformylase

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 48.21Å b: 42.19Å c: 101.67Å
α: 90° β: 98.67° γ: 90°
R-values:
R R work R free
0.231 0.231 0.265
Expression system: Escherichia coli

Quick links

Citations

12 review citations

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

3 mentions without citation

Structure and activity of human mitochondrial peptide deformylase, a novel cancer target.
Escobar-Alvarez et al. (2009)
2 more