1dfi

X-ray diffraction
2.09Å resolution

X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD

Released:

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:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 261 amino acids
Theoretical weight: 27.76 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0AEK4 (Residues: 2-262; Coverage: 100%)
Gene names: JW1281, b1288, envM, 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
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX7.2
Spacegroup: P21
Unit cell:
a: 74Å b: 81.2Å c: 79Å
α: 90° β: 92.9° γ: 90°
R-values:
R R work R free
0.162 0.162 not available
Expression system: Escherichia coli BL21