Combining crystallographic information and an aspherical-atom data bank in the evaluation of the electrostatic interaction energy in an enzyme–substrate complex: influenza neuraminidase inhibition

Acta Cryst. (2009). D65, 485–499 (doi.org/10.1107/S0907444909009433)

Since the electron density of a particular atom is determined by its surroundings, atomic electron densities are transferable to other sites with identical bonding environments. The University at Buffalo Databank of aspherical atomic densities is used to synthesize the electron densities of the influenza neuraminidase enzyme and 70 different inhibitors to evaluate the electrostatic enzyme–inhibitor interaction energy at an accuracy well beyond that of the point-charge approximation. Relative electrostatic interaction energies of the inhibitors and the effect of the Arg292→Lys mutation are calculated.

P.M. Dominiak, A. Volkov, A.P. Dominiak, K.N. Jarzembska and P. Coppens