Sandbox 50: Difference between revisions
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The <scene name='Sandbox_50/Ak_secondary_structure/1'>secondary_structure</scene> of the protein contains 12 alpha helices (yellow) and 7 beta sheets (green). This secondary structure is held together by <scene name='Sandbox_50/Ak_hydrogen_bonds/1'>hydrogen_bonds</scene>, which are anti-parallel between the beta sheets. | The <scene name='Sandbox_50/Ak_secondary_structure/1'>secondary_structure</scene> of the protein contains 12 alpha helices (yellow) and 7 beta sheets (green). This secondary structure is held together by <scene name='Sandbox_50/Ak_hydrogen_bonds/1'>hydrogen_bonds</scene>, which are anti-parallel between the beta sheets. | ||
==Residues== | |||
The amino acid <scene name='Sandbox_50/Ak_hydrophobic_residues/1'>hydrophobic_residues</scene> of ADK, seen in gray, is buried in the interior of the protein. While the <scene name='Sandbox_50/Ak_hydrophilic_residues1/1'>hydrophilic_residues</scene>, all the charged and polar side chains (purple), are either on the surface of the protein or exposed in the active site. | |||
<scene name='Sandbox_50/Ak_hydrophilic_residues/1'>hydrophilic_residues</scene> | |||
<scene name='Sandbox_50/Ak_alpha_helices/1'>alpha_helices</scene> | <scene name='Sandbox_50/Ak_alpha_helices/1'>alpha_helices</scene> | ||
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<scene name='Sandbox_50/Ak_water/1'>water</scene> | <scene name='Sandbox_50/Ak_water/1'>water</scene> | ||
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<scene name='Sandbox_50/Ak_water4/1'>water4</scene> | <scene name='Sandbox_50/Ak_water4/1'>water4</scene> | ||
<scene name='Sandbox_50/Ak_water5/1'>water5</scene> | <scene name='Sandbox_50/Ak_water5/1'>water5</scene> | ||
<scene name='Sandbox_50/Ak_ligand1/1'>ligand1</scene> | <scene name='Sandbox_50/Ak_ligand1/1'>ligand1</scene> | ||
<scene name='Sandbox_50/Ak_ligand3/1'>ligand3</scene> | <scene name='Sandbox_50/Ak_ligand3/1'>ligand3</scene> | ||
Revision as of 19:40, 18 October 2012
Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013.
DescriptionAdenylate Kinase, also known as ADK, is an enzyme that catalyzes the reversible transfer of phosphate between ATP and AMP. It plays an important role in cell maintenance and cell growth being involved with energy metabolism, signaling, and nucleotide synthesis. The enzyme is found in many different organisms, and the following images shows the structure of Adenylate kinase from Yersinia pestis, also known as yeast. StructureAdenylate kinase is made up of 214 amino acids, and the backbone of the protein can be seen on the right in light blue surrounding the non-hydrolysable substrate analogue (red). The secondary_structure of the protein contains 12 alpha helices (yellow) and 7 beta sheets (green). This secondary structure is held together by hydrogen_bonds, which are anti-parallel between the beta sheets. ResiduesThe amino acid hydrophobic_residues of ADK, seen in gray, is buried in the interior of the protein. While the hydrophilic_residues, all the charged and polar side chains (purple), are either on the surface of the protein or exposed in the active site.
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