Sandbox Reserved 801

From Proteopedia

Jump to: navigation, search
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

Succinyl-CoA synthetase

Succinyl CoA-synthetase

Drag the structure with the mouse to rotate


is an enzyme that plays a key role in the citric acid cycle by catalyzing the reaction of succinyl-CoA + NDP + Pi <-> succinate + CoA + NTP. The isoform shown here is from Sus scrofa and utilizes GTP. Other isoforms utilize ATP. Succinyl-CoA synthetase is a dimer composed of two chains, alpha and beta. The alpha chain is shown in green and the beta chain is shown in blue. The is composed of alpha helices (blue), beta sheets (yellow), and nonrepetitive sequences. stabilizes the structure of the protein and is evident especially in the alpha helices and beta sheets. The hydrogen bonds, shown in black, run down the length of the helices and between the strands of the beta sheets. There are relatively more hydrogen bonds between the sidechains on the exterior portion of the protein than the interior. This is largely a result of more hydrophobic occuring in the interior and more hydrophilic residues occuring on the exterior, where they can interact with water. is highest on the outside of the protein and the region between the two subunits. This crystal structure was determined to have 3 : GTP (red), K+ (purple), and PO4- (purple). The potassium and GTP are held in close proximity, where the potassium sits between the terminal phosphate groups, allowing the positive and negative charges to stabilize each other. This site is surrounded by positively charged residues that further complement the negative charges of the phosphates. The (Glu217(A), Glu204(B), and Tyr116(B)) are shown in green.

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_801"
Personal tools