› 4j0e

X-ray diffraction
1.6Å resolution

Crystal structure of 3-hydroxyacyl-CoA dehydrogenase from Caenorhadbitis elegans in P1 space group

Released:
DOI: 10.2210/pdb4j0e/pdb
PDB entry 4j0e coloured by chain, front view.
PDB entry 4j0e coloured by chain, side view.
PDB entry 4j0e coloured by chain, top view.
Source organism: Caenorhabditis elegans
Primary publication:
Purification, crystallization and preliminary crystallographic analysis of 3-hydroxyacyl-CoA dehydrogenase from Caenorhabditis elegans.
Xu Y, Sun F
Acta Crystallogr Sect F Struct Biol Cryst Commun 69 515-9 (2013)
PMID: 23695566

Function and Biology Details

Reaction catalysed: 
(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152706 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable 3-hydroxyacyl-CoA dehydrogenase F54C8.1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 320 amino acids
Theoretical weight: 34.71 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: P34439 (Residues: 1-298; Coverage: 100%)
Gene name: F54C8.1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P1
Unit cell:
a: 55.709Å b: 55.215Å c: 56.066Å
α: 80.45° β: 75.58° γ: 72.42°
R-values:
R R work R free
0.226 0.223 0.27
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Dimerization interface of 3-hydroxyacyl-CoA dehydrogenase tunes the formation of its catalytic intermediate.
Xu et al. (2014)