2fhs

X-ray diffraction
2.7Å resolution

Structure of Acyl Carrier Protein Bound to FabI, the Enoyl Reductase from Escherichia Coli

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:

Structure analysis Details

Assemblies composition:
hetero hexamer (preferred)
homo tetramer
PDBe Complex ID:
PDB-CPX-141283 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI Chains: A, B
Molecule details ›
Chains: A, B
Length: 262 amino acids
Theoretical weight: 27.89 KDa
Source organism: Escherichia coli str. K-12 substr. W3110
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEK4 (Residues: 1-262; Coverage: 100%)
Gene names: JW1281, b1288, envM, fabI
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain
Acyl carrier protein Chain: C
Molecule details ›
Chain: C
Length: 78 amino acids
Theoretical weight: 8.65 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6A8 (Residues: 1-78; Coverage: 100%)
Gene names: JW1080, acpP, b1094
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P6522
Unit cell:
a: 127.74Å b: 127.74Å c: 206.73Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.224 0.263
Expression system: Escherichia coli