PDBe 1qsg

X-ray diffraction
1.75Å resolution

CRYSTAL STRUCTURE OF ENOYL REDUCTASE INHIBITION BY TRICLOSAN

Released:
Source organism: Escherichia coli

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

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 265 amino acids
Theoretical weight: 28.18 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEK4 (Residues: 1-262; Coverage: 100%)
Gene names: JW1281, b1288, envM, fabI
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P1
Unit cell:
a: 73.733Å b: 82.077Å c: 84.177Å
α: 89.54° β: 87.43° γ: 77.77°
R-values:
R R work R free
0.172 0.172 0.215
Expression system: Escherichia coli