PDBe 1ps9

X-ray diffraction
2.2Å resolution

The Crystal Structure and Reaction Mechanism of E. coli 2,4-Dienoyl CoA Reductase

Source organism: Escherichia coli

Function and Biology Details

Reaction catalysed:
Trans-2,3-didehydroacyl-CoA + NADP(+) = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
2,4-dienoyl-CoA reductase Chain: A
Molecule details ›
Chain: A
Length: 671 amino acids
Theoretical weight: 72.63 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P42593 (Residues: 2-672; Coverage: 100%)
Gene names: JW3052, b3081, fadH, ygjL
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand FMN 1 x FMN

Cofactor: Ligand FAD 1 x FAD

Cofactor: Ligand NAP 1 x NAP
3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200, APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 65.601Å b: 109.227Å c: 110.304Å
α: 90° β: 90° γ: 90°
R R work R free
0.205 0.203 0.243
Expression system: Escherichia coli