Chiral recognition mechanism of cellobiohydrolase Cel7A for ligands based on the β‐blocker propranolol: The effect of explicit water molecules on binding and selectivities

Proteins are useful chiral selectors. In order to understand the recognition mechanism and discrimination, binding of (R)- (S)-enantiomers a series designed amino alcohol inhibitors based on propranolol cellobiohydrolase Cel7A (Trichoderma reesei) has been studied more closely. X-ray crystal structures were determined protein complex with strongest analogue. The combination structural data, thermodynamic data from capillary electrophoresis microcalorimetry experiments computational modelling give clearer insight into origin enantioselectivity its opposite signature. new used in molecular flexible dockings analogues using program Glide. results indicated that several water molecules active site essential for docking (R)-enantiomers but not (S)-enantiomers. discussed relation enantiomeric discrimination enzyme. Both dissociation constants (Kd values) thermodynamical included show effects modifications ligand enthalpy entropy enantioselectivity.