3g5p

X-ray diffraction
1.7Å resolution

Structure and activity of human mitochondrial peptide deformylase, a novel cancer target

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-190753 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide deformylase, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 183 amino acids
Theoretical weight: 20.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HBH1 (Residues: 64-243; Coverage: 74%)
Gene names: PDF, PDF1A
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 24-ID-C
Spacegroup: C2
Unit cell:
a: 116.332Å b: 77.825Å c: 111.041Å
α: 90° β: 107.93° γ: 90°
R-values:
R R work R free
0.162 0.161 0.187
Expression system: Escherichia coli