› 1ws0

X-ray diffraction
1.7Å resolution

Structure analysis of peptide deformylase from Bacillus cereus

Released:
DOI: 10.2210/pdb1ws0/pdb
PDB entry 1ws0 coloured by chain, front view.
PDB entry 1ws0 coloured by chain, side view.
PDB entry 1ws0 coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Structure analysis of peptide deformylase from Bacillus cereus.
Moon JH, Park JK, Kim EE
Proteins 61 217-20 (2005)
PMID: 16049914

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182458 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide deformylase 1 Chain: A
Molecule details ›
Chain: A
Length: 156 amino acids
Theoretical weight: 17.5 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q819U0 (Residues: 1-156; Coverage: 100%)
Gene names: BC_3865, def1
Sequence domains: Polypeptide deformylase
Structure domains: Peptide deformylase

Ligands and Environments

1 bound ligand:
Ligand NI 1 x NI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: P212121
Unit cell:
a: 44.33Å b: 42.802Å c: 84.806Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.2 0.223
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

Trapping conformational states along ligand-binding dynamics of peptide deformylase: the impact of induced fit on enzyme catalysis.
Fieulaine et al. (2011)
3 more

1 mention without citation

Bacterial protein structures reveal phylum dependent divergence.
Shortridge et al. (2011)