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Trp-493 binding pocket in a homology model of αENaC knuckle domain in α1βα2γ tetramer. Indole ring of Trp-493 is embedded inside the knuckle domain's cavity. Stabilizing phenylalanines Phe-280 and Phe-503 geometrically confine the pocket. Additional polar interactions stabilize the Trp-493's binding pose like γVal-322 from the neighboring γ-subunit. Trp-493 is connected to the pore-lining residue Arg-492 through the peptide chain.
