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X-ray diffraction
2.8Å resolution

Crystals of Peptide Deformylase from Plasmodium falciparum with Ten Subunits per Asymmetric Unit Reveal Critical Characteristics of the Active Site for Drug Design

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

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide deformylase Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 183 amino acids
Theoretical weight: 21.82 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8I372 (Residues: 63-239; Coverage: 73%)
Gene name: PF3D7_0907900
Sequence domains: Polypeptide deformylase
Structure domains: Peptide deformylase

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P41
Unit cell:
a: 121.263Å b: 121.263Å c: 177.272Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.231 0.296
Expression system: Escherichia coli BL21(DE3)