3uov

X-ray diffraction
2.04Å resolution

Crystal Structure of OTEMO (FAD bound form 1)

Released:
Model geometry
Fit model/data

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-124785 (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

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P21
Unit cell:
a: 59.007Å b: 139.983Å c: 67.569Å
α: 90° β: 98.38° γ: 90°
R-values:
R R work R free
0.192 0.19 0.24
Expression system: Escherichia coli BL21(DE3)