1nhw

X-ray diffraction
2.35Å resolution

Crystal Structure Analysis of Plasmodium falciparum enoyl-acyl-carrier-protein reductase

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero octamer
PDBe Complex ID:
PDB-CPX-189625 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Enoyl-acyl carrier reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 229 amino acids
Theoretical weight: 25.74 KDa
Source organism: Plasmodium falciparum
Expression system: Bacteria
UniProt:
  • Canonical: Q9BH77 (Residues: 97-325; Coverage: 56%)
Gene name: FabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain
Enoyl-acyl carrier reductase Chains: C, D
Molecule details ›
Chains: C, D
Length: 60 amino acids
Theoretical weight: 6.83 KDa
Source organism: Plasmodium falciparum
Expression system: Bacteria
UniProt:
  • Canonical: Q9BH77 (Residues: 366-425; Coverage: 15%)
Gene name: FabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: Enoyl acyl carrier protein reductase

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 133.365Å b: 133.365Å c: 83.862Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.232
Expression system: Bacteria