› 1bsz

X-ray diffraction
1.9Å resolution

PEPTIDE DEFORMYLASE AS FE2+ CONTAINING FORM (NATIVE) IN COMPLEX WITH INHIBITOR POLYETHYLENE GLYCOL

Released:
DOI: 10.2210/pdb1bsz/pdb
PDB entry 1bsz coloured by chain, front view.
PDB entry 1bsz coloured by chain, side view.
PDB entry 1bsz coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Iron center, substrate recognition and mechanism of peptide deformylase.
Becker A, Schlichting I, Kabsch W, Groche D, Schultz S, Wagner AF
Nat Struct Biol 5 1053-8 (1998)
PMID: 9846875

Function and Biology Details

Reaction catalysed: 
Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141367 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide deformylase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 168 amino acids
Theoretical weight: 19.23 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6K3 (Residues: 2-169; Coverage: 99%)
Gene names: JW3248, b3287, def, fms
Sequence domains: Polypeptide deformylase
Structure domains: Peptide deformylase

Ligands and Environments

3 bound ligands:
Ligand FE 3 x FE
Ligand 2PE 3 x 2PE
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-18
Spacegroup: C2
Unit cell:
a: 141Å b: 63.4Å c: 86.8Å
α: 90° β: 120.6° γ: 90°
R-values:
R R work R free
0.197 0.197 0.247
Expression system: Escherichia coli

Quick links

Citations

13 review citations

The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium.
Imlay JA. (2013)
12 more

2 mentions without citation

Targeting Metalloenzymes for Therapeutic Intervention.
Chen et al. (2019)
1 more