› 5k3i

X-ray diffraction
2.68Å resolution

Crystal structure of Acyl-CoA oxidase-1 in Caenorhabditis elegans complexed with FAD and ATP

Released:
DOI: 10.2210/pdb5k3i/pdb
PDB 5k3i coloured by chain and viewed from the front.
PDB 5k3i coloured by chain and viewed from the side.
PDB 5k3i coloured by chain and viewed from the top.
Source organism: Caenorhabditis elegans
Primary publication:
Structural characterization of acyl-CoA oxidases reveals a direct link between pheromone biosynthesis and metabolic state in Caenorhabditis elegans.
Zhang X, Li K, Jones RA, Bruner SD, Butcher RA
Proc Natl Acad Sci U S A 113 10055-60 (2016)
PMID: 27551084

Function and Biology Details

Reaction catalysed: 
Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-coenzyme A oxidase acox-1.1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 684 amino acids
Theoretical weight: 77.5 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: O62140 (Residues: 1-674; Coverage: 100%)
Gene names: F08A8.1, acox-1, acox-1.1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 8 x FAD
2 bound ligands:
Ligand ATP 8 x ATP
Ligand MG 8 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 152.339Å b: 141.501Å c: 154.968Å
α: 90° β: 116.76° γ: 90°
R-values:
R R work R free
0.218 0.217 0.232
Expression system: Escherichia coli

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Citations

2 review citations

Ascaroside Pheromones: Chemical Biology and Pleiotropic Neuronal Functions.
Park et al. (2019)
1 more