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Dimethylarginine Dimethylaminohydrolase in Bos Tarus bound with Zinc at pH 9.0Dimethylarginine Dimethylaminohydrolase in Bos Tarus bound with Zinc at pH 9.0

This is a default text for your page Colton Junod/Sandbox 1. 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 Inhibitors Zinc at pH 9.0 In DDAH, Zinc (Zn2+) acts as an endogenous inhibitor and prevents normal NOS activity. The Zn(II)-binding site is located inside the protein’s active site, which makes it a competitive inhibitor. It was found that Cys273, His172, Glu77, Asp78, and Asp 268 all play a role in the binding of Zn(II). Cys273 directly coordinates with the Zn(II) ion in the active site while the other significant residues stabilize the ion via hydrogen bonding interactions with water molecules in the active site. Depending on pH, His172 can change conformations and use the imidazole group to directly coordinate the Zn(II) ion. Cys273, which is conserved between bovine and humans, is the key active site residue that coordinates Zn(II). Zinc-cysteine complexes have been found to be important mediators of protein catalysis, regulation, and structure. Cys273 and the water molecules stabilize the Zn(II) ion in a tetrahedral environment. The Zn(II) dissociation constant is 4.2 nM which is consistent with the nanomolar concentrations of Zn(II) in the cells, thus provides more evidence for the regulatory use of Zn(II) by DDAH. Structure Figure Legend Structural highlights This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

spinqualitylabelsall models Dimethylarginine Dimethylaminohydrolase in Complex with Zinc at pH 9.0 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image