Phytanoyl-CoA dioxygenase Structure

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Originally, the structure of our protein was experimentally defined (by Zhang, Z., Butler, D., McDonough, M.A et.al.) via X-ray diffraction.

Name - Phytanoyl-CoA dioxygenase (PHYHD1)
Classification - Oxidoreductase
Resolution (Amstrongs) - 1.90
R-Value - 0.221 (obs, relatively low)
Space Group - P 3.1 2 1
Unit Cell Paramters (Amstrongs) - a = 91.97, b = 91.97, c = 81.61
Unit Cell Angles - alpha = 90.00, beta = 90.00, gamma = 120.00

Using Pymol the image was visualized in a few different ways to get a general overview of the protein. The stick structures tended to be clutered so a surface rendering was done and a cartoon depiction. These are below.

Figure 1
This image was taken from behind the pocket of the molecule (cartoon).

Figure 2
The pocket can be seen here in a cartoon depiction.

Figure 3
The surface was rendered and the image from behind the pocket was taken again.

Figure 4
This is the surface rendering of the pocket.

There are high levels of steric hinderance if the approaching ligand comes from behind the molecule (figure 1, figure 3).

There is a large hole in the structure of our protein (figure 2, figure 4). As steric hinderance is low and the surface area is maximized at this position, it would seem that this area should encompass the binding sites of our protein, or at least be the location of some form of interaction. The fact such a definitive hole in the structure of the protein exists lead us to investigate further properties around this region.

Figure 1
Showing the topology of the protein. Reproduced from the European Bioinformatics Institute,
http://www.ebi.ac.uk/thornton-srv/databases/pdbsum/2opw/domA01.gif

Figure 2
Showing another topology of the protein. Reproduced from the European Bioinformatics Institute,
http://www.ebi.ac.uk/