Sandbox Reserved 800

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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

PBD: 2AKZ

Catalytic Residus: E 166; H 189; E 209; V 240; K 342; H 370; A 393;

Ligands: G37; A38; S39; T40; I42; H157; Q165; E166; E209; S248; E249; Q297; K342; R371; S372

Metal Ligand Binding Sites: S39; Q165; E166; D244; E242 D317; L340 K342; K393

This Enzyme is a Dimer

Enzyme Reaction 2-phospho-D-glycerate <--> phosphoenolpyruvate + H2O

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

This is . Isn't it pretty! :) This is with the helixes and sheets represented in different colors.This scene shows the of Enolate. The hydrophobic residues are shown in grey. are shown in purple while the beta-sheets are shown in yellow. The way that the hydrogen bonds are set up shows that the beta-sheets are parallel in nature, however, there are also anti-parallel beta-sheets at other portions of the molecule. is shown in red, with the enzyme in a grey and the ligand is in green. The water is mostly located on the outer edge of the Enolate with some clustering in and around the ligand binding site. The is shown here. The ligand (Malate) is interacting with mostly polar residues to stabilize malate binding in the pocket with hydrogen bonds. There are also some non-polar side chains that are not involved in hydrogen bonding, but and important in the shape and stability of the binding pocket. The