Team:ITESM-CEM/Oxoacyl

From 2014.igem.org

(Difference between revisions)
Line 76: Line 76:
      
      
<p><img src="https://static.igem.org/mediawiki/2014/0/08/Imagenes_enzimas_modelado-4.jpg" align="left" width="590" height="403" hspace="20"></p><br><br><br>
<p><img src="https://static.igem.org/mediawiki/2014/0/08/Imagenes_enzimas_modelado-4.jpg" align="left" width="590" height="403" hspace="20"></p><br><br><br>
-
<br><br><br>
 
-
<br><br><br>
 
-
<br><br><br>
 
-
<br><br><br>
 
-
<br><br><br>
 
-
<br><br><br>
 
<br><br><br>
<br><br><br>
<br><br><br>
<br><br><br>

Revision as of 14:21, 2 October 2014

TEC-CEM | Modeling

ITESM-CEM | Enzy7-K me

Modeling 3325

 

Oxoacyl Reductase

This tridimensional model was obtained with the I-TASSER software. It has a -0.70 C-score which makes it, out of the 5 predicted models, the more plausible to be the actual tridimensional conformation of the protein.

The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.
















Physicochemical Characteristics

When a BLAST was performed several results were obtained which fulfilled a similarity of over 95%, all of them were registered and characterized Oxoacetil reductases from other organisms. The structural comparison was made with a 3-oxoacyl-acyl carrier protein reductase from Staphylococcus aureus. As it can be observed in the figures bellow the tridimensional structure are fairly similar. An interesting piece of information is that most of the registered Oxoacetil reductases work in homo 4-mers.