Sandbox Reserved 789
From Proteopedia
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<Structure load='1CSC' size='500' frame='true' align='right' caption='Citrate Synthase' scene='Insert optional scene name here' /> | <Structure load='1CSC' size='500' frame='true' align='right' caption='Citrate Synthase' scene='Insert optional scene name here' /> | ||
Citrate synthase exists in nearly all cells, and is responsible for catalyzing the first reaction in the citric acid cycle: the condensation of acetyl-CoA and oxaloacetate to form citrate. Citrate synthase consists of 437 amino acids, which are organized in to two identical subunits. Citrate synthase is considered a <scene name='56/563201/Homodimer/1'>homodimer</scene> of a single amino acid chain monomer, this makes up its tertiary structure. Each subunit consists of 20 alpha-helicies. Alpha-helicies make up the majority of the enzymes <scene name='56/563201/Secondary_structure/3'>secondary structure</scene>, with few beta sheets. The a- helicies are represented in purple, while the B- sheets are in blue. | Citrate synthase exists in nearly all cells, and is responsible for catalyzing the first reaction in the citric acid cycle: the condensation of acetyl-CoA and oxaloacetate to form citrate. Citrate synthase consists of 437 amino acids, which are organized in to two identical subunits. Citrate synthase is considered a <scene name='56/563201/Homodimer/1'>homodimer</scene> of a single amino acid chain monomer, this makes up its tertiary structure. Each subunit consists of 20 alpha-helicies. Alpha-helicies make up the majority of the enzymes <scene name='56/563201/Secondary_structure/3'>secondary structure</scene>, with few beta sheets. The a- helicies are represented in purple, while the B- sheets are in blue. | ||
- | The <scene name='56/563201/Hydrogen_bonds/1'> | + | The <scene name='56/563201/Hydrogen_bonds/1'>picture</scene> depicts the hydrogens bonds in the backbone. |
- | + | Here the <scene name='56/563201/Hydrophobic_residues/1'>hydrophobic residues</scene> are depicted, as well as the <scene name='56/563201/Hydrophilic_residues/1'>hydrophilic residues</scene>. | |
- | + | ||
<scene name='56/563201/Water_interactions/1'>Water molecules are</scene> represented by the blue spheres. A ligand is represented in purple. | <scene name='56/563201/Water_interactions/1'>Water molecules are</scene> represented by the blue spheres. A ligand is represented in purple. | ||
<scene name='56/563201/Ligand_interactions/1'>Ligand interactions</scene> are depicted in ball and stick and the rest of the protein is in ribbon. | <scene name='56/563201/Ligand_interactions/1'>Ligand interactions</scene> are depicted in ball and stick and the rest of the protein is in ribbon. | ||
<scene name='56/563201/Catalytic_residues/1'>Catalytic residues</scene> are shown in black. | <scene name='56/563201/Catalytic_residues/1'>Catalytic residues</scene> are shown in black. |
Revision as of 00:17, 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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Citrate synthase exists in nearly all cells, and is responsible for catalyzing the first reaction in the citric acid cycle: the condensation of acetyl-CoA and oxaloacetate to form citrate. Citrate synthase consists of 437 amino acids, which are organized in to two identical subunits. Citrate synthase is considered a of a single amino acid chain monomer, this makes up its tertiary structure. Each subunit consists of 20 alpha-helicies. Alpha-helicies make up the majority of the enzymes , with few beta sheets. The a- helicies are represented in purple, while the B- sheets are in blue. The depicts the hydrogens bonds in the backbone. Here the are depicted, as well as the . represented by the blue spheres. A ligand is represented in purple. are depicted in ball and stick and the rest of the protein is in ribbon. are shown in black.