Figure 3 - full size


Figure 3.
Fig. 3. Active site of PWA with bound acarbose and zinc (PWA·Ac/Zn; A and B), Tris (PWA·Tris; C and D), and zinc (PWA·Zn; E and F). A, C, and E, structures of active site residues in the presence of bound ligands. Each F[o] F[c] difference electron density map (green) in the absence of ligands (A, acarbose; C, Tris; and E, zinc) is contoured at 2.0, 2.0, and 4.5 , respectively. In E, the anomalous difference peak (red) is contoured at 3.7 . B, D, and F, schematic representations of the ligands bound to the active site. Hydrogen bonds are shown by dashed lines. Zinc ions and solvent molecules are shown as green and gray spheres, respectively. Solvent molecules mediating protein-inhibitor interactions are indicated in B, D, and F; for clarity, Tyr62, Phe^159, and Tyr199 are not shown.

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 9875-9884) copyright 2003.