Sandbox 42: Difference between revisions
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<Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate kinase' scene='Scene 1' /> | <Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate kinase' scene='Scene 1' /> | ||
==Introduction== | ==Introduction== | ||
Adenylate kinase is a protein that is found in the bacterium ''yersinia pestis''. It consists of two chains, <scene name='Sandbox_42/Wes_-_1ake/1'>Chain A</scene> and Chain B. The two chains are identical and so structural elements can be examined by focusing on one chain. | Adenylate kinase is a protein that is found in the bacterium ''yersinia pestis''. It consists of two chains, <scene name='Sandbox_42/Wes_-_1ake/1'>Chain A</scene> and Chain B. The two chains are identical and so structural elements can be examined by focusing on one chain. The space filling section of the protein is the ligand, which is bound to the active site in this representation. | ||
==Structural Elements== | ==Structural Elements== | ||
Revision as of 02:48, 15 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.
IntroductionAdenylate kinase is a protein that is found in the bacterium yersinia pestis. It consists of two chains, Chain A and Chain B. The two chains are identical and so structural elements can be examined by focusing on one chain. The space filling section of the protein is the ligand, which is bound to the active site in this representation. Structural ElementsThe secondary structure is highlighted here, with alpha helices (shown in green) and beta sheets (blue). Hydrogen bonds are shown in black. These bonds show that the beta sheets are connected in parallel, as the hydrogen bonds are angled and not parallel to one another. hydrophobic residues in gray polar and charged residues in brown Water in yellow - secondary structure Water in yellow - ball/stick ligand and interacting side chains are shown here in stick/wire representation, with the rest of the protein semi-transparent. Active site residues in purple |