Sandbox Reserved 1697

Text To Be Displayed

This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

7KIR

spinqualitylabelsall models Inositol plyphosphate 1-phosphatase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page Sandbox 1677. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Function of your protein The function of 7KIR is dephosphorylating inositol, the substrate is IP2 and the product is IP. The protein studied was taken from Bos taurus but is present in many different organisms, including humans. Important amino acids In the protein seen in the paper there is a mutation at residue 54, causing an aspartic acid to change to an alanine. The catalytic amino acids are Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313. Structural highlights This protein is a mutation of 1INP, it has thirteen structural elements. The amino acids in the bind to the substrate all participate in hydrogen bonding to the substrate and ligand. The structure is 77% helix and 23% beta sheet, the betta sheets allow for twisting of the molecule so that the ligand better fits within the enzyme. The helices allow for hydrogen bonding throughout to stabilize the structure with assistance from metal ions; specifically magnesium ions. Other important features The ligand of the protein is known as D-MYO-INOSITOL-1,4-BISPHOSPHATE, with a PDB ID of 2IP. The cyclic structure of the ligand could possibly assist with binding the substrate, the hydrogen bonding with various amino acids allows for many interactions with the enzyme. This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.