› 1rl4

X-ray diffraction
2.18Å resolution

Plasmodium falciparum peptide deformylase complex with inhibitor

Released:
DOI: 10.2210/pdb1rl4/pdb
PDB entry 1rl4 coloured by chain, front view.
PDB entry 1rl4 coloured by chain, side view.
PDB entry 1rl4 coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
An improved crystal form of Plasmodium falciparum peptide deformylase.
Robien MA, Nguyen KT, Kumar A, Hirsh I, Turley S, Pei D, Hol WG
Protein Sci 13 1155-63 (2004)
PMID: 15010544

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184653 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptide deformylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 188 amino acids
Theoretical weight: 22.27 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8I372 (Residues: 59-236; Coverage: 74%)
Gene name: PF3D7_0907900
Sequence domains: Polypeptide deformylase
Structure domains: Peptide deformylase

Ligands and Environments

3 bound ligands:
Ligand CO 2 x CO
Ligand BRR 2 x BRR
Ligand BL5 2 x BL5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P65
Unit cell:
a: 102.317Å b: 102.317Å c: 118.339Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.197 0.212
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The plastid-derived organelle of protozoan human parasites as a target of established and emerging drugs.
Wiesner et al. (2005)
1 more

10 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
9 more