Sandbox Reserved 790
From Proteopedia
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The <scene name='56/563202/Hydrophilic_residues/1'>hydrophilic and hydrophobic residues</scene> are shown here. The hydrophilic residues are shown in blue, and the hydrophobic residues are shown in green. | The <scene name='56/563202/Hydrophilic_residues/1'>hydrophilic and hydrophobic residues</scene> are shown here. The hydrophilic residues are shown in blue, and the hydrophobic residues are shown in green. | ||
<scene name='56/563202/Water_and_non_water/1'>Water molecules</scene> are shown within the structure in green, and the non-water parts of the enzyme are shown in purple. | <scene name='56/563202/Water_and_non_water/1'>Water molecules</scene> are shown within the structure in green, and the non-water parts of the enzyme are shown in purple. | ||
+ | The <scene name='56/563202/Ligands/1'>ligands</scene> in pyruvate kinase are highlighted in green. The interacting groups are made up of charged residues like aspartate, glutamate, lysine, and histidine. |
Revision as of 13:15, 17 October 2013
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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The of pyruvate kinase shows alpha helices (pink) surrounding beta sheets (blue) in a tetramer. The are shown here. The hydrophilic residues are shown in blue, and the hydrophobic residues are shown in green. are shown within the structure in green, and the non-water parts of the enzyme are shown in purple. The in pyruvate kinase are highlighted in green. The interacting groups are made up of charged residues like aspartate, glutamate, lysine, and histidine.