PDBe 5i7v

X-ray diffraction
2.6Å resolution

Crystal structure of B. pseudomallei FabI in complex with NAD and PT02

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:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 276 amino acids
Theoretical weight: 29.33 KDa
Source organism: Burkholderia pseudomallei
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3HP34 (Residues: 1-263; Coverage: 100%)
Gene names: BP1026B_I1187, fabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 3 x NAD
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: I222
Unit cell:
a: 69.62Å b: 111.95Å c: 262.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.221 0.28
Expression system: Escherichia coli