Cholesterol oxidase
This tridimensional model was obtained with the I-TASSER software. It has a - 1.34 C-score which makes it, out of the 5 predicted models, the more plausible to be the actual tridimensional conformation of the protein.
![](https://static.igem.org/mediawiki/2014/6/61/Colox1.jpg)
The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.
![](https://static.igem.org/mediawiki/2014/0/08/Imagenes_enzimas_modelado-4.jpg)
Physicochemical Characteristics
The following pictures are the structural comparison between two different secuences of the cholesterol oxidase from Chromobacterium sp.
Logically, the results showed a 100% similarity when a BLAST was performed. The only discrepancies found exist on the ends of the protein. Were in figure 4 it can be appreciated a red helix that belongs to the cholesterol oxidase expressed by the iGEM team ITESM.CEM. It is noteworthy that this enzyme works as a monomer.