Sandbox 40: Difference between revisions
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==Adenylate Kinase== | |||
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<Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Insert optional scene name here' /> | |||
< | The <scene name='Sandbox_40/Adenylate_kinase_1ake_a/6'>secondary structure</scene> of adenylate kinase shows the alpha helices (green) and the beta sheets (purple)surrounding the non-hydrolysable substrate analogue. Backbone <scene name='Sandbox_40/Adenylate_kinase_1ake_a/4'>H-bonds</scene> are shown (orange). <scene name='Sandbox_40/Adenylate_kinase_1ake_a_sheets/1'>Beta sheets</scene> are highlighted here with the antiparallel (crimson) and the more numerous parallel sheets (remaining violet). <scene name='Sandbox_40/Adenylate_kinase_1ake_a/8'>Hydrophobic residues</scene> can be seen as gray "wire-frame" structures, and <scene name='Sandbox_40/Adenylate_kinase_1ake_a/10'>Hydrophilic residues</scene> 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, <scene name='Sandbox_40/Adenylate_kinase_1ake_a/11'>solvent accessibility</scene> is predicted for water (aqua). The ligand is highlighted (orange). <scene name='Sandbox_40/Adenylate_kinase_1ake_a/12'>Interactions with the ligand</scene> 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 <scene name='Sandbox_40/Adenylate_kinase_1ake_a/15'>active site</scene> is shown in yellow and represents data found in sequence analysis using PDBsum. Residues: R123-R156-R167-D158-D159-K13. | ||
Latest revision as of 04:30, 19 October 2012
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.
The secondary structure of adenylate kinase shows the alpha helices (green) and the beta sheets (purple)surrounding the non-hydrolysable substrate analogue. Backbone H-bonds are shown (orange). Beta sheets are highlighted here with the antiparallel (crimson) and the more numerous parallel sheets (remaining violet). Hydrophobic residues can be seen as gray "wire-frame" structures, and Hydrophilic residues 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, solvent accessibility is predicted for water (aqua). The ligand is highlighted (orange). Interactions with the ligand 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 active site is shown in yellow and represents data found in sequence analysis using PDBsum. Residues: R123-R156-R167-D158-D159-K13. |
