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 <scene name='56/563202/Hydrophilic_residues/2'>hydrophilic residues</scene> are highlighted in blue; these are found on the outer surface of the protein since they interact with the solvent. The <scene name='56/563202/Hydrophobic_esidues/1'>hydrophobic residues</scene> are highlighted in green and are found on the interior of the protein, away from the solvent. | The <scene name='56/563202/Hydrophilic_residues/1'>hydrophilic and hydrophobic residues</scene> are shown here. The <scene name='56/563202/Hydrophilic_residues/2'>hydrophilic residues</scene> are highlighted in blue; these are found on the outer surface of the protein since they interact with the solvent. The <scene name='56/563202/Hydrophobic_esidues/1'>hydrophobic residues</scene> are highlighted in green and are found on the interior of the protein, away from the solvent. | ||
<scene name='56/563202/Water_and_non_water/1'>Water molecules</scene> (the solvent with which the protein is interacting) 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> (the solvent with which the protein is interacting) 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_by_chain/1'>ligands</scene> in pyruvate kinase are highlighted by chain: chain A ligands are in white, chain B ligands are in light purple, chain C ligands are in blue, and chain D ligands are in green. The interacting groups are made up of charged residues like aspartate, glutamate, lysine, and histidine | + | The <scene name='56/563202/Ligands_by_chain/1'>ligands</scene> in pyruvate kinase are highlighted by chain: chain A ligands are in white, chain B ligands are in light purple, chain C ligands are in blue, and chain D ligands are in green. The interacting groups are made up of charged residues like aspartate, arginine, glutamate, lysine, and histidine. |
Revision as of 15:28, 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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Pyruvate kinase is an enzyme that is utilized in process of glycolysis. Its function within glycolysis is to catalyze the last step of the reaction, in which the second ATP and pyruvate are generated. The catalysis happens by transferring the phosphate group from phosphoenolpyruvate to ADP. This specific pyruvate kinase is found in the liver of humans. The of pyruvate kinase shows alpha helices (pink) surrounding beta sheets (blue). Its structure in general has a beta-barrel domain-like fold, and its tertiary structure is tetrameric, with four different domains. The are shown here. The are highlighted in blue; these are found on the outer surface of the protein since they interact with the solvent. The are highlighted in green and are found on the interior of the protein, away from the solvent. (the solvent with which the protein is interacting) 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 by chain: chain A ligands are in white, chain B ligands are in light purple, chain C ligands are in blue, and chain D ligands are in green. The interacting groups are made up of charged residues like aspartate, arginine, glutamate, lysine, and histidine.
