3oje

X-ray diffraction
3.02Å resolution

Crystal Structure of the Bacillus cereus Enoyl-Acyl Carrier Protein Reductase (Apo form)

Released:
Source organism: Bacillus cereus ATCC 14579
Primary publication:
Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus.
Biochem Biophys Res Commun 400 517-22 (2010)
PMID: 20800575

Function and Biology Details

Reaction catalysed:
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-182530 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI Chain: A
Molecule details ›
Chain: A
Length: 256 amino acids
Theoretical weight: 27.77 KDa
Source organism: Bacillus cereus ATCC 14579
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q81GI3 (Residues: 1-256; Coverage: 100%)
Gene names: BC_1216, fabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: C2221
Unit cell:
a: 83.148Å b: 95.528Å c: 67.109Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.269 0.269 0.27
Expression system: Escherichia coli BL21(DE3)