› 1is2

X-ray diffraction
2.2Å resolution

Crystal Structure of Peroxisomal Acyl-CoA Oxidase-II from Rat Liver

Released:
DOI: 10.2210/pdb1is2/pdb
PDB entry 1is2 coloured by chain, front view.
PDB entry 1is2 coloured by chain, side view.
PDB entry 1is2 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase.
Nakajima Y, Miyahara I, Hirotsu K, Nishina Y, Shiga K, Setoyama C, Tamaoki H, Miura R
J Biochem 131 365-74 (2002)
PMID: 11872165

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 domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139805 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisomal acyl-coenzyme A oxidase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 661 amino acids
Theoretical weight: 74.78 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07872 (Residues: 1-661; Coverage: 100%)
Gene names: Acox, Acox1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 72.03Å b: 91.501Å c: 214.477Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.26
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Biochemistry and genetics of inherited disorders of peroxisomal fatty acid metabolism.
Van Veldhoven PP. (2010)
4 more

11 mentions without citation

Building collagen IV smart scaffolds on the outside of cells.
Brown et al. (2017)
10 more