Sandbox 40
From Proteopedia
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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' /> | ||
| - | 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). The <scene name='Sandbox_40/Adenylate_kinase_1ake_a/5'>antiparallel beta sheets</scene> are highlighted (cyan). <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). | + | 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). The <scene name='Sandbox_40/Adenylate_kinase_1ake_a/5'>antiparallel beta sheets</scene> are highlighted (cyan). <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) and anionic residues (red). |
Revision as of 02:21, 19 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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The of adenylate kinase shows the alpha helices (green) and the beta sheets (purple)surrounding the non-hydrolysable substrate analogue. Backbone are shown (orange). The are highlighted (cyan). 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) and anionic residues (red).
