Sandbox 38
From Proteopedia
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==Residues== | ==Residues== | ||
The protein consists of <scene name='Sandbox_38/Adenylate_kinase_2o_structure/4'>hydrophobic</scene> and <scene name='Sandbox_38/Adenylate_kinase_2o_structure/5'>hydrophilic</scene> residues, highlighted in gray and red, respectively. | The protein consists of <scene name='Sandbox_38/Adenylate_kinase_2o_structure/4'>hydrophobic</scene> and <scene name='Sandbox_38/Adenylate_kinase_2o_structure/5'>hydrophilic</scene> residues, highlighted in gray and red, respectively. | ||
| + | |||
| + | ==Water Accessibility== | ||
| + | The protein has certain <scene name='Sandbox_38/Adenylate_kinase_2o_structure/6'>water accessibility</scene> (water shown in blue, the enzyme shown in white), since water can't interact with all of it. Water also interacts with some of the <scene name='Sandbox_38/Adenylate_kinase_2o_structure/7'>internal residues</scene>. Waters are and aren't places. | ||
| + | |||
| + | ==Ligand== | ||
| + | Some <scene name='Sandbox_38/Adenylate_kinase_2o_structure/8'>residues contact the ligand</scene>. Although not all of the highlighted residues contact the ligand, most of them do. Cationic side chains are shown in blue, whereas anionic side chains are shown in red. What kind of side chains interact with non-hydrolysable substrate. The <scene name='Sandbox_38/Adenylate_kinase_2o_structure/10'>catalytic residues</scene> are shown in green. | ||
Revision as of 20:40, 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. |
Contents |
Secondary Structure
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The of adenylate kinase is really cool. There are two ; the alpha-helices are highlighted in light green and the beta-sheets are highlighted in dark green. The are shown in yellow. They may be parallel or anti-parallel.
Residues
The protein consists of and residues, highlighted in gray and red, respectively.
Water Accessibility
The protein has certain (water shown in blue, the enzyme shown in white), since water can't interact with all of it. Water also interacts with some of the . Waters are and aren't places.
Ligand
Some . Although not all of the highlighted residues contact the ligand, most of them do. Cationic side chains are shown in blue, whereas anionic side chains are shown in red. What kind of side chains interact with non-hydrolysable substrate. The are shown in green.
