Sandbox 35: Difference between revisions

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<Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Insert optional scene name here' />
<Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Insert optional scene name here' />
==Adenylate Kinase==
==Adenylate Kinase==
Adenylate kinase, also known as "ADK", is an enzyme which speeds up the reaction that includes the interconversion of adenine nucleotides. The protein's flexibility allows it to bind to certain substrates known as ligands.  
Adenylate kinase, also known as "ADK", is an enzyme which speeds up the reaction that includes the interconversion of adenine nucleotides. The protein's flexibility allows it to bind to certain substrates known as ligands. Adenylate kinase is known for influencing cellular energy homeostasis. 


==Structure==
==Structure==
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==Adenylate Kinase and The Ligand==
==Adenylate Kinase and The Ligand==
The ligand(dark pink) in the center of the protein has specific residues surrounding it that are also known as the <scene name='Sandbox_35/Secondary_with_ligand_in_cente/1'>ligand contacts</scene>. These residues have polar-charged side chains, which stabilize the ligand. The ligand in Adenylate kinase is a molecule which is able to bind to the protein's specific active site.
The ligand(dark pink) in the center of the protein has specific residues surrounding it that are also known as the <scene name='Sandbox_35/Secondary_with_ligand_in_cente/1'>ligand contacts</scene>. These residues have polar-charged side chains, which stabilize the ligand. The ligand in Adenylate kinase is a molecule which is able to bind to the protein's specific active site.
==Catalytic Residues==
The <scene name='Sandbox_35/Secondary_catalytic_residues/1'>catalytic residues</scene> (black) are found in the center of the protein, lining the active site where the ligand binds. These residues, also known as "active site residues", help with recognition of the ligand. The ligand binds with the protein in various ways: hydrogen bonds, hydrophobic interactions, temporary covalent interactions, or a mixture of the mentioned methods. The catalytic residues assist the reaction by acting as proton donors or acceptors. In the big picture, all of this helps the enzyme protein lower the activation energy of the ligand to speed up the reaction efficiently.