X-ray diffraction
1.85Å resolution

Crystal structure of a peptide deformylase from Burkholderia multivorans in complex with actinonin

Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Peptide deformylase Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 20.91 KDa
Source organism: Burkholderia multivorans ATCC 17616
Expression system: Escherichia coli BL21(DE3)
  • Canonical: A0A0H3KPJ9 (Residues: 1-177; Coverage: 100%)
Gene names: BMULJ_01994, def
Sequence domains: Polypeptide deformylase
Structure domains: Peptide deformylase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: I222
Unit cell:
a: 39.12Å b: 70.54Å c: 140.51Å
α: 90° β: 90° γ: 90°
R R work R free
0.169 0.165 0.203
Expression system: Escherichia coli BL21(DE3)