Sandbox 38

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. Adenylate kinase is an enzyme that catalyzes the reaction ATP + AMP = 2ADP. It consists of two identical subunits, A (shown in blue) and B (shown in green). For simplicity's sake, only the A chain will be shown in consequent green links. Basic structural elements spinqualitylabelsall models Adenylate Kinase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Like many proteins, the secondary structure of adenylate kinase consists of two elements: alpha-helices (shown in light green) and beta-sheets (shown in dark green). Non-repetitive structural elements are shown in light blue/gray. In addition to the regular hydrogen bonding that causes the secondary structure of the protein, additional hydrogen bonding is present in the backbone of adenylate kinase (shown in yellow), which also contributes to the overall stability/folding of the molecule. A additional, significant factor in the structural stability/folding of the molecule is the polarity of the amino acid residues. The hydrophobic (nonpolar) residues are shown in gray, while the hydrophilic (polar/charged) residues are shown in red. Water Accessibility The protein has certain water accessibility (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 internal residues. Waters are and aren't places. Ligand Some residues contact the ligand. 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 catalytic residues are shown in green.