We identified two complementary conformational search platforms: Induced fit docking (IFD) and accelerated molecular dynamics (aMD) (Fig. ). IFD is a MM-based docking protocol that is widely utilized by medicinal chemists to approximate the docking pose of a ligand and the concomitant repositioning of nearby enzyme residues. We generated ensembles of the [EL] by hijacking the IFD protocol to describe both ligand and enzyme repositioning. In addition to the robust [EL] structural data generated by IFD, we integrated IFD into our workflow because it is easily implemented and does not require sophisticated computing hardware. To complement the IFD workflow, we desired a scalable platform to rapidly scan enzyme mutant space. Therefore, we employed aMD, which allows for flexibility in the entire enzyme, to quickly assemble apo-enzyme structures that represent the dynamic ensemble. These structures were paired with free ligand conformational ensembles from MM/DFT. Since enzymes and substrates are assembled separately in the aMD sampling platform, this approach is applicable to large enzyme-ligand matrices and has potential for virtual screening.