Sandbox Reserved 793
From Proteopedia
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==Introduction== | ==Introduction== | ||
The protein <scene name='56/563205/Aconitase-_unedited/1'>aconitase</scene> holds a vital role as a protein in the citric acid cycle. As a catalyst enzyme, aconitase facilitates the reaction that converts citrate to isocitrate, the product used by isocitrate dehydrogenase. It does this through its ability to form both a citrate and an isocitrate complex. | The protein <scene name='56/563205/Aconitase-_unedited/1'>aconitase</scene> holds a vital role as a protein in the citric acid cycle. As a catalyst enzyme, aconitase facilitates the reaction that converts citrate to isocitrate, the product used by isocitrate dehydrogenase. It does this through its ability to form both a citrate and an isocitrate complex. | ||
| - | The <scene name='56/563205/Helices_and_sheets/1'>secondary structure</scene> of aconitase contains both alpha helices (green) and beta sheets (blue) surrounding the ligands. | + | ==Structural Features== |
| + | The <scene name='56/563205/Helices_and_sheets/1'>secondary structure</scene> of aconitase contains both alpha helices (green) and beta sheets (blue) surrounding the ligands. The tertiary structure of the protein places its active site in the middle. Since aconitase exists as a monomer, not quaternary structure is present. | ||
<scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone. | <scene name='56/563205/Hydrogen_bonds/1'>Hydrogen bonds</scene> are shown in brown throughout the protein's backbone. | ||
<scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein. | <scene name='56/563205/Hydrophobic/1'>Hydrophobic residues</scene> (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein. | ||
<scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water. | <scene name='56/563205/Hydrophillic_and_hydrophobic/1'>Hydrophilic residues</scene> and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water. | ||
| + | ==Ligand Interactions== | ||
<scene name='56/563205/Interactions/1'>ligand interactions </scene> | <scene name='56/563205/Interactions/1'>ligand interactions </scene> | ||
<scene name='56/563205/Interactions_close_up/1'>interactions close up</scene> | <scene name='56/563205/Interactions_close_up/1'>interactions close up</scene> | ||
<scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene> | <scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene> | ||
Revision as of 21:35, 18 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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Introduction
The protein holds a vital role as a protein in the citric acid cycle. As a catalyst enzyme, aconitase facilitates the reaction that converts citrate to isocitrate, the product used by isocitrate dehydrogenase. It does this through its ability to form both a citrate and an isocitrate complex.
Structural Features
The of aconitase contains both alpha helices (green) and beta sheets (blue) surrounding the ligands. The tertiary structure of the protein places its active site in the middle. Since aconitase exists as a monomer, not quaternary structure is present. are shown in brown throughout the protein's backbone. (light purple) are present throughout the secondary structure of aconitase, primarily in regions tucked close to the center of the protein. and charged residues(dark purple) are present in the protein in areas where in it is typically exposed to water.
Ligand Interactions
