› 1w6u

X-ray diffraction
1.75Å resolution

Structure of human DECR ternary complex

Released:
DOI: 10.2210/pdb1w6u/pdb
PDB entry 1w6u coloured by chain, front view.
PDB entry 1w6u coloured by chain, side view.
PDB entry 1w6u coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase: enzyme-ligand interactions in a distinctive short-chain reductase active site.
Alphey MS, Yu W, Byres E, Li D, Hunter WN
J Biol Chem 280 3068-77 (2005)
PMID: 15531764

Function and Biology Details

Reaction catalysed: 
A (3E)-3-enoyl-CoA + NADP(+) = a (2E,4E)-2,4-dienoyl-CoA + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172560 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 302 amino acids
Theoretical weight: 32.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q16698 (Residues: 34-335; Coverage: 90%)
Gene names: DECR, DECR1, SDR18C1
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

2 bound ligands:
Ligand NAP 4 x NAP
Ligand HXC 4 x HXC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 63.281Å b: 131.658Å c: 70.849Å
α: 90° β: 92.64° γ: 90°
R-values:
R R work R free
0.229 0.227 0.268
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Medium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes.
Kavanagh et al. (2008)
3 more

9 mentions without citation

Natural products from thioester reductase containing biosynthetic pathways.
Mullowney et al. (2018)
8 more