Sandbox Reserved 793
From Proteopedia
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<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/ | + | <scene name='56/563205/Hydrophobic_and_philic-_better/1'>Hydrophilic </scene> and charged residues(navy blue) are present in the protein in areas where in it is typically exposed to water. |
==Ligand Interactions== | ==Ligand Interactions== | ||
Several <scene name='56/563205/Interactions/1'>ligand interactions </scene> allow aconitase to form the citrate complex necessary for the citric acid cycle to occur. | Several <scene name='56/563205/Interactions/1'>ligand interactions </scene> allow aconitase to form the citrate complex necessary for the citric acid cycle to occur. | ||
Looking at these <scene name='56/563205/Interactions_close_up/1'>interactions close up</scene> it is easier to see the different components: the iron-sulfate complex (red and yellow), citrate anion (orange), and oxygen atom (blue). | Looking at these <scene name='56/563205/Interactions_close_up/1'>interactions close up</scene> it is easier to see the different components: the iron-sulfate complex (red and yellow), citrate anion (orange), and oxygen atom (blue). | ||
The <scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene> (dark green) allow the enzyme to properly bind the ligand and perform the function. | The <scene name='56/563205/Catalyst_enz/1'>catalyst enzymes</scene> (dark green) allow the enzyme to properly bind the ligand and perform the function. | ||
Revision as of 21:59, 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(navy blue) are present in the protein in areas where in it is typically exposed to water.
Ligand Interactions
Several allow aconitase to form the citrate complex necessary for the citric acid cycle to occur. Looking at these it is easier to see the different components: the iron-sulfate complex (red and yellow), citrate anion (orange), and oxygen atom (blue). The (dark green) allow the enzyme to properly bind the ligand and perform the function.
