Sandbox Reserved 1845

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This Sandbox is Reserved from March 18 through September 1, 2025 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson and Mark Macbeth at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1828 through Sandbox Reserved 1846.

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

LCC Crystalized Structure of Leaf-branch compost cutinase

spinqualitylabelsall models Original Structure of LCC 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 '. 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. Introduction 2-HE(MET)3 Structural Overview Catalytic Triad Catalytic Triad Location Ligand Binding Site Figure 1 Mutations F243 F243 I243 F243W The original side chain is phenylalanine side chain, is located 3.6 Angstroms from the ligand. There are two main mutations isoleucine and tryptophan. Isoleucine is a smaller molecule and makes a tighter bond in the ligand, with the distance being 3.0 Angstrom. This allows for more efficient interactions with the ligand, likely improving substrate binding and catalytic efficiency. The other is tryptophan, which is a bulkier side chain, which does have a slightly shorter difference of 3.2 Angstroms, while being a larger side chain. The effect that is has is more based on that tryptophan is a nitrogen-containing aromatic ring, which offers new interactions with the substrate, which could also affect enzyme's binding and catalytic properties. These two mutations both lead to an increase in catalytic activity from the mutation, F243I had a 27.5% increase and F243W had an 17.5% increase, when compared to the wild-type variant. T96 T96 The original side chain is threonine and is mutated with a methionine. This is really a mutation that increases thermostability. The wild-type variant has a melting point of 84.7 degree Celsius. The mutation of methionine, is a larger, more hydrophobic side chain, and would contribute to stabilization of the protein's core by increasing hydrophobic interactions. The stronger internal interactions help the enzyme to maintain its folded structure more efficiently at elevated temperatures. Which is shown by the M96 mutation having a melting point of 87.4 degree Celsius. Y127 Y127 G127 The original side chain is tyrosine, and is has a mutation to glycine. Like the T96M mutation, it also increases thermostability of the protein, with this mutation Y127G having a melting point of 87.0 degree Celsius. The mutation replaces tyrosine, a bulky, rigid aromatic side chain to glycine, which is the smallest amino acid. This mutation leads to allowing greater flexibility for the protein. By reducing steric hindrance and releasing some strain in the protein structure, allowing for it to be more flexible and more stable at higher temperatures. N246 N246 S283 & D238 S283 & D238 C283 & C238 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.