3oic

X-ray diffraction
2.2Å resolution

Crystal Structure of Enoyl-ACP Reductases III (FabL) from B. subtilis (apo form)

Released:
Source organism: Bacillus subtilis

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-159777 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADPH] FabL Chains: A, D
Molecule details ›
Chains: A, D
Length: 258 amino acids
Theoretical weight: 28.28 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P71079 (Residues: 1-250; Coverage: 100%)
Gene names: BSU08650, fabL, yfhR, ygaA
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21212
Unit cell:
a: 85.211Å b: 93.426Å c: 66.324Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.226 0.282
Expression system: Escherichia coli