2o2y

X-ray diffraction
2.2Å resolution

The crystal structure of P. 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
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-acyl carrier reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 349 amino acids
Theoretical weight: 39.63 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BH77 (Residues: 84-432; Coverage: 85%)
Gene name: FabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P21
Unit cell:
a: 88.184Å b: 82.368Å c: 94.824Å
α: 90° β: 90.77° γ: 90°
R-values:
R R work R free
0.202 0.2 0.246
Expression system: Escherichia coli