two positively charged residues</scene> Arg 100 and Arg 139.
Glu96 and Glu129.
Two which include Phe191 Val141 and
Ala93 for one, and the other patch includes Phe146 Val126 and Leu108. A look at the picture shows that there are hydrophobic patches (in gray) "above" and "below" the ligand ,negatively charged residues "above-right" and "below-left" of the ligand and positively charges on the "right" and "left" of it.
This symmetry can be exploited, a symmetric molecule can bind the same interface in two different ways thus increasing the "chance" of binding which means better binding affinity.>
