3oif

X-ray diffraction
2.6Å resolution

Crystal Structure of Enoyl-ACP Reductases I (FabI) from B. subtilis (complex with NAD and TCL)

Released:
Source organism: Bacillus subtilis

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-547390 (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: 266 amino acids
Theoretical weight: 28.98 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P54616 (Residues: 1-258; Coverage: 100%)
Gene names: BSU11720, fabI, yjbW
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: P212121
Unit cell:
a: 64.098Å b: 83.655Å c: 203.547Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.276
Expression system: Escherichia coli BL21(DE3)