Figure 5: The differences in the drug-binding cleft between the two molecules in the OM+ structure.
From: Structural basis for drug-induced allosteric changes to human β-cardiac myosin motor activity
(a) The A chain conformation of the drug-binding site showing the interacting residues. (b) The B chain conformation of the drug-binding site. OM interacts with the same set of residues in both conformations of the binding cleft. The principal change between OM-A and OM-B is the rotation of the converter domain indicated by the arrow in b. In this view the converter domain moves up and towards the viewer, shifting the position of both N711 and R712. The fluoro-benzyl and methy-pyidinyl rings of OM rotate between OM-A and OM-B conformations as does the amino-carbamoyl group linking them. This maintains the H-bond to N711 and the shielding of the E497-R712 salt bridge. The carboxymethyl-piperazine is buried deep in the cleft and interacts with S118 and F121 of the β1 and β2 strands of the seven-stranded β-sheet.
