Figure 1 - full size


Figure 1.
Figure 1. Contacts of IDD 594 with AR and NADP^+. (a) 3D view of inhibitor contacts. View of the inhibitor-binding site down the barrel axis with the semitransparent representation of AR surface. The active site cleft (marked A), is occupied by the inhibitor (stick only; color code: C = gray, N = blue, O = red, F = pink, S = orange, Br = green) and surrounded by the catalytic residues His 110, Tyr 48, and the coenzyme NADP^+. The residues within 3.9 Å and NADP^+ are shown (balls and sticks). The specificity pocket between Leu 300, Phe 122, and Trp 111 (marked S) is occupied by the brominated aromatic ring of the inhibitor. (b) Scheme of IDD 594 and its contacts. Red dashed lines show contacts between 3.5 and 3.0 Å, and blue dashed lines show contacts <3.0 Å. The exact values are given in Table IV.

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2004, 55, 792-804) copyright 2004.