Sandbox Reserved 797

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This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807.

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spinqualitylabelsall models Succinate dehydrogenase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Succinate dehydrogenase

This is the of succinate dehydrogenase, a component of the citric acid cycle responsible for conversion of succinate to fumarate. It is a tetrameric protein found on the inner membrane of the mitochondria.

As can be seen in the image above, the of the enzyme is composed of alpha helices (purple) and beta sheets (pink) connected by nonrepetitive structure.

Most secondary structure is held in place by backbone (orange), as illustrated here. To make bonds more obvious, they are also shown for the second copy of the protein in the dimer. As can be seen in the pink beta sheets, the sheets run primarily _____. No disulfide bonds are present in the structure.

Both residues are present in succinate dehydrogenase. Again, both the full structure and the residues alone are shown.

Solvating water is present around multiple chains (white) in succinate dehydrogenase. Shown here is (blue) solvating chain A.

Ligands interact with succinate dehydrogenase in a multitude of locations for a veritable plethora of reasons. Shown here is one in the A chain (lime green). This non-hydrolyzable ligand interacts with uncharged side chains; namely, valine.

One (yellow) is found in succinate dehydrogenase, located in the A chain. Please note that the active site consists of one valine residue, so it is very tiny here. It is located in the upper right of the enzyme in a non-rotating view.