› 2op0

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reaction catalysed: 
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189626 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-acyl carrier reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 338 amino acids
Theoretical weight: 38.35 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BH77 (Residues: 96-425; Coverage: 80%)
Gene name: FabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
2 bound ligands:
Ligand SO4 1 x SO4
Ligand 7PC 1 x 7PC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P43212
Unit cell:
a: 132.305Å b: 132.305Å c: 82.911Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.187 0.274
Expression system: Escherichia coli

Quick links

Citations

7 review citations

New medicines to improve control and contribute to the eradication of malaria.
Wells et al. (2009)
6 more

2 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)
1 more