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

This is the of Phosphofructokinase. It contains 10 . The pattern of shows there to be a mixture of parallel and anti-parallel β-sheets. The parallel sheets can be identified by the angled hydrogen bonds, while the anti-parallel sheets contain straight hydrogen bonds. A display of the hydrophobic (orange) and hydrophilic (blue) shows that the hydrophobic groups are predominantly in the center of the protein, while the hydrophilic groups occupy the periphery and the active site. associate with the surface and active site of the enzyme. The position of the water molecules corresponds with the of the hydrophilic side chains, which is to be expected. The line the inside of the active site pocket, and consist of a variety of hydrophilic amino acids such as lysine, glutamic acid, and histidine. The consist of four side chains, an alanine, an aspartic acid, and two glycines. In honor of this year's Nobel laureates, the space-filling model of phosphofructokinase with its associated waters can be seen .