Sandbox 50
From Proteopedia
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==Description== | ==Description== | ||
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| - | Adenylate 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, | + | Adenylate Kinase, also known as ADK, is an phosphotransfer 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 reaction, ATP + AMP = 2ADP, The enzyme is found in many different organisms, but the following images shows the structure of Adenylate kinase from Yersinia pestis, also known as yeast. |
==Structure== | ==Structure== | ||
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==Residues== | ==Residues== | ||
| - | The | + | The <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 on the surface of the protein and exposed. |
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| + | ==Solvent== | ||
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| + | <scene name='Sandbox_50/Ak_water5/1'>water5</scene> | ||
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| + | ==Active Site== | ||
| + | The active site is where the ligand/substrate binds to the enzyme to be catalyzed. In ADK, the <scene name='Sandbox_50/Ak_ligand3/1'>ligand3</scene>, in | ||
| + | <scene name='Sandbox_50/Ak_catalytic_residues/1'>catalytic_residues</scene> | ||
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<scene name='Sandbox_50/Ak_ligand1/1'>ligand</scene> | <scene name='Sandbox_50/Ak_ligand1/1'>ligand</scene> | ||
<scene name='Sandbox_50/Ak_ligand2/1'>ligand2</scene> | <scene name='Sandbox_50/Ak_ligand2/1'>ligand2</scene> | ||
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<scene name='Sandbox_50/Ak_solvent1/1'>solvent1</scene> | <scene name='Sandbox_50/Ak_solvent1/1'>solvent1</scene> | ||
<scene name='Sandbox_50/Ak_solvent2/1'>solvent2</scene> | <scene name='Sandbox_50/Ak_solvent2/1'>solvent2</scene> | ||
<scene name='Sandbox_50/Ak_water3/1'>water3</scene> | <scene name='Sandbox_50/Ak_water3/1'>water3</scene> | ||
<scene name='Sandbox_50/Ak_water4/1'>water4</scene> | <scene name='Sandbox_50/Ak_water4/1'>water4</scene> | ||
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<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> | ||
Revision as of 19:55, 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. |
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Contents |
Description
Adenylate Kinase, also known as ADK, is an phosphotransfer 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 reaction, ATP + AMP = 2ADP, The enzyme is found in many different organisms, but the following images shows the structure of Adenylate kinase from Yersinia pestis, also known as yeast.
Structure
Adenylate kinase is made up of 214 amino acids, and the of the protein can be seen on the right in light blue surrounding the non-hydrolysable substrate analogue (red). The of the protein contains 12 alpha helices (yellow) and 7 beta sheets (green). This secondary structure is held together by , which are anti-parallel between the beta sheets.
Residues
The of ADK, seen in gray, is buried in the interior of the protein. While the , all the charged and polar side chains (purple), are on the surface of the protein and exposed.
Solvent
Active Site
The active site is where the ligand/substrate binds to the enzyme to be catalyzed. In ADK, the , in
