Sandbox 50

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 Description Adenylate Kinase, also known as ADK, is an phosphotransfer enzyme that catalyzes the reversible transfer of phosphate between ATP and AMP. It plays an important role in cell maintenance and cell growth being involved with energy metabolism, signaling, and nucleotide synthesis. The reaction, ATP + AMP = 2ADP, The enzyme is found in many different organisms, but the following images shows the structure of Adenylate kinase from Yersinia pestis, also known as yeast. Structure Adenylate kinase is made up of 214 amino acids, and the backbone of the protein can be seen on the right in light blue surrounding the non-hydrolysable substrate analogue (red). The secondary_structure of the protein contains 12 alpha helices (yellow) and 7 beta sheets (green). This secondary structure is held together by hydrogen_bonds, which are anti-parallel between the beta sheets. Residues The hydrophobic_residues of ADK, seen in gray, is buried in the interior of the protein. While the hydrophilic_residues, all the charged and polar side chains (purple), are on the surface of the protein and exposed. Solvent water5 Active Site The active site is where the ligand/substrate binds to the enzyme to be catalyzed. In ADK, the ligand3, in catalytic_residues hydrophilic_residues alpha_helices beta_sheets water water2 ligand ligand2 solvent1 solvent2 water3 water4 ligand1