Sandbox 48

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. spinqualitylabelsall models Adenylate Kinase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Adenylate Kinase Adenylate kinase (or ADK) is an enzyme known to catalyze the interconversion of adenosine triphosphate (ATP) and adenosine monophosphate (AMP) to two molecules of adenosine diphosphate (ADP), and vice versa. This enzyme is imporant for cellular energy homeostasis because the need for ADP. ADP is required for oxidative phosphorylation, an important step in multiple metabolic pathways. Secondary Structure in Chain A We will be examining the structure of chain A in adenylate kinase. The secondary structures of Chain A of adenylate kinase includes alpha-helices (green), and beta-sheets (blue). The location of the hydrogen bonds within the secondary structure demonstrates how the alpha-helices and beta-sheets are hydrogen bonded. Within these structures the hydrophobic residues (purple) are located closest on the inside of the enzyme. The hydrophillic residues (green), which are those that are charged or polar, are on the outward face of the enzyme. Solvent Accessibility To assess the solvent accessibility of adenylate kinase, water molecules (purple) are shown on the molecule. These are the spaces in the protein that are capable of being accessed by solvent. Solvent accumulates near the center of the molecule, and is found on the outward chains like the alpha helices. The ligand (green) is highlighted to show that the water molecules surround the ligand in the middle of the ligand, but not by the ends. Ligand Interaction There are charged residues that interact with the ligand, or make up the interaction site. The positively charged (blue) residues of the enzyme interact with the negatively charged (red) residues of the ligand.