› 3lt2

X-ray diffraction
2.5Å 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 analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189641 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-ACP reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 329 amino acids
Theoretical weight: 37.24 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BJJ9 (Residues: 96-424; 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 2 x NAD
1 bound ligand:
Ligand FT3 2 x FT3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 131.018Å b: 131.018Å c: 82.954Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.248
Expression system: Escherichia coli

Quick links

Citations

2 review citations

From crystal to compound: structure-based antimalarial drug discovery.
Drinkwater et al. (2014)
1 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