Sandbox Reserved 782

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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 Phosphofructokinase from Listeria Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Phosphofructokinase

This is the of Phosphofructokinase. The Purple designates the alpha helices...finish description

The bulk of this proteins structure is made up of the alpha helices are in yellow and the beta sheets are in grey. In addition the three green balls represent the three Mg atoms, the internal compound is ATP and the small grey and red group off to the side is the glycerol.

is a very important part of protein structure shape and stability. The hydrogen bonds of phosphofructokinase are designated by the orange dotted lines throughout the structure. Phosphofructokinase contains both anti-parallel and parallel sheets, which are identified by parallel hydrogen bonds and angled hydrogen bonds respectively.

One of the most important determining factors of protein structure lies in hydrophobic interactions between the with the surrounding environment. The hydrophobic residues are designated with light green while the hydrophobic residues are shown in blue. As would be expected the majority of the hydrophobic residues are located at the center of the protein where they are shielded from the hydrophobic environment.