The Na+/K+ ATPase pump transports:
Sodium-potassium pump is archetypal P-type ATPase maintaining electrochemical gradients vital for volume control and excitability. Each cycle hydrolyzes one ATP to ADP and phosphate, driving conformational shift from E1 high Na+ affinity inward to E2 low affinity outward via phosphorylated Asp369 intermediate. In E1 facing cytosol, cavity binds three sodium ions, triggering autophosphorylation. Transition to E2-P exposes cavity extracellularly where Na+ affinity drops, sodium released and potassium sites exposed. Two extracellular potassium ions bind with high affinity in E2-P, inducing dephosphorylation returning to E1 where potassium released inside due to low affinity. Net result is outward movement of three Na+ and inward two K+ per ATP, generating net outward positive current and inside-negative potential around minus seventy millivolts, preventing swelling and providing high internal K+ favoring ribosome function. This gradient fuels secondary transporters like Na+/Ca2+ and Na+/H+ exchangers and action potential recovery. Cardiac glycosides ouabain and digoxin inhibit by binding E2-P state, raising intracellular Na+.
Ref: Skou & Esmann, Journal of Bioenergetics 1992: Na+,K+-ATPase Stoichiometry – 3 Na+ out, 2 K+ in.