Figure shows the predicted binding mode of the designed ligand (Molecule #1) and the residues from the target that interact with it, demonstrating that the shape of the designed ligand is complementary to that of that target's active site. The following residues were observed at distances of less than 3.0A from the designed molecule in the predicted pose: Y97, Q99, I100, S102, G164, S165, N168, F217, H218, R220, E293, S297, E298, D326, V328, Q329, K357. All of these residues, except 97-102 and 297 are part of the active site of GABA-T. The reference set of residues at the active site of GABA-T were obtained from the structure of pig GABA-T inactivated with a substrate analog, obtained from X-ray diffraction data . Studies of mechanism based inhibitors of pig GABA-T have demonstrated that residues G164, S165, F217, H218, R220, D326, V328 and K357 play critical roles in the catalytic process , and all of these residues are at a distance of less than 3.0A from the designed molecule in the predicted pose for binding to human GABA-T. The mechanistic studies were carried out on pig GABA-T and the reported values were converted to the human GABA-T numbering used in this work for comparison by using pairwise sequence alignment of human and pig GABA-T.