5i9m

X-ray diffraction
2.25Å resolution

Crystal structure of B. pseudomallei FabI in complex with NAD and PT408

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)
PDBe Complex ID:
PDB-CPX-101892 (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: BESSY BEAMLINE 14.1
Spacegroup: I222
Unit cell:
a: 69.029Å b: 111.217Å c: 260.695Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.251 0.281
Expression system: Escherichia coli