› 3uox

X-ray diffraction
1.96Å resolution

Function and Biology Details

Reaction catalysed: 
((1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA + O(2) + NADPH = ((2R)-3,3,4-trimethyl-6-oxo-3,6-dihydro-1H-pyran-2-yl)acetyl-CoA + NADP(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-124784 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 545 amino acids
Theoretical weight: 61.45 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: H3JQW0 (Residues: 1-545; Coverage: 100%)
Gene names: camG, otemo
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

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: APS BEAMLINE 31-ID
Spacegroup: P21
Unit cell:
a: 67.318Å b: 92.54Å c: 93.35Å
α: 90° β: 103.27° γ: 90°
R-values:
R R work R free
0.192 0.19 0.23
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Microbial monoterpene transformations-a review.
Marmulla et al. (2014)
3 more

1 mention without citation

Cloning, Baeyer-Villiger biooxidations, and structures of the camphor pathway 2-oxo-Δ(3)-4,5,5-trimethylcyclopentenylacetyl-coenzyme A monooxygenase of Pseudomonas putida ATCC 17453.
Leisch et al. (2012)