Our electric field calculations show that the residues surrounding the selectivity filter set the electrostatic environment in Na v 1.7's pore. However, we also see a significant contribution from water. Previous work extensively describes water alignment in protein channels, although most studies focus on smaller channels with narrow pores. Water alignment reports on the electrostatic potential and can be critical to ion permeation and channel selectivity. In this section, we investigate the structural and dynamical properties of the water molecules in Na v 1.7's pore and interpret the result in the context of our electric field calculations.