1dff

X-ray diffraction
2.88Å resolution

PEPTIDE DEFORMYLASE

Released:
Source organism: Escherichia coli
Primary publication:
Crystal structure of the Escherichia coli peptide deformylase.
Biochemistry 36 13904-9 (1997)
PMID: 9374869

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide deformylase Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.8 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6K3 (Residues: 2-165; Coverage: 97%)
Gene names: JW3248, b3287, def, fms
Sequence domains: Polypeptide deformylase
Structure domains: Peptide deformylase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P6122
Unit cell:
a: 55.35Å b: 55.35Å c: 230.92Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.184 0.289
Expression system: Escherichia coli