Sandbox Reserved 807

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spinqualitylabelsall models Enolase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. 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

. This shows the alpha-helices in blue, and the beta-sheets in orange, as well as the non-repetitive structure in white

has lots of cool alpha-helices

is displayed here in red.

Because the beta-sheets are parallel, the H-bonds are not direct or straight, and therefore not as strong.

are shown in gray. These residues prefer little to no contact with water, and so typically hide in the interior of the protein

are shown in purple. These residues prefer contact with water, and so typically appear on the surface of the protein

surrounding Enolase only reacts with the hydrophilic residues of the protein and forces the hydrophobic residues into the interior to minimize contact with them and so water can increase its own entropy.

is displayed in yellow. The majority of the residues binding with the Ligand include Serine, Glutamic acid, and Aspartic acid.

are shown here in lime green. These are the residues of the enzyme's active site that are reported to also interact with the non-hydrolysable substrate.

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