Sandbox 40

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Adenylate Kinase

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.

Adenylate Kinase

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The of adenylate kinase shows the alpha helices (green) and the beta sheets (purple)surrounding the non-hydrolysable substrate analogue. Backbone are shown (orange). are highlighted here with the antiparallel (crimson) and the more numerous parallel sheets (remaining violet). can be seen as gray "wire-frame" structures, and are represented by the red "wire-frame" structures. Hydrophilic residues are considered to be any polar or charged residues in the protein structure. Using Jpred, is predicted for water (aqua). The ligand is highlighted (orange). are highlighted in this scene with cationic residues (blue), anionic residues (red), and histidine residues (light blue). The side chains are largely positive lysine and argnine residues. Due to the role Adenylate kinase plays in catalyzing the conversion of 2ADP molecules to 1ATP and 1AMP, it is useful for the active site to bind well to a negatively charged ligand. The is shown in yellow and represents data found in sequence analysis using PDBsum. Residues: R123-R156-R167-D158-D159-K13.

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