Sandbox 40: Difference between revisions

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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).

Sandbox 40: Difference between revisions

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 <!-- PLEASE ADD YOUR CONTENT BELOW 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).