The extracellular part of the sodium-potassium pump contains the glycosylated beta-subunit. These subunits combine to form a αβγ-complex whose crystal structure has been obtained by the vapor-diffusion method in hanging drops. The rest of the alpha-subunit is predominantly composed of alpha helices with a few random coils. The alpha subunit contains three areas in its amino acid sequence forming beta sheets. The alpha subunit is involved in ATP hydrolysis and the binding of cations, while the beta subunit is critical to stability and trafficking of the sodium-potassium pump to the membrane (8). The alpha subunit consists of residues 19 to 1016, the beta subunit consists of residues 28 to 73 and the gamma-subunit consists of residues 23 to 51 in a model of its crystal structure. The sodium-potassium pump contains three subunits : an alpha, beta, and gamma subunit. The sodium-potassium pump described in detail in the following paragraphs is in the E2 product state (E2⋅MgF 4 2- ) (1). The pump returns to its original E1 state when the bound K + ions are released into the cytosol (8). The phosphate group is released at this stage by hydrolysis with water. When the Na + ions are released into the extracellular space, 2 K + ions are bound to the pump in its E2 state. In the E1 conformation, the pump is phosphorylated by ATP and 3 Na + ions bind to their active sites in the pump. During one ATP hydrolysis cycle, the sodium-potassium pump undergoes two conformational changes between an E1 and E2 state. P-type ATPases function through the phosphorylation of an intermediate that catalyzes ATP hydrolysis. The electrical gradient that is created by the movement of Na + and K + affects stimulation of nerve and muscle cells. The concentration of Na + ions inside cells must be regulated to counteract cell lysis. The sodium-potassium pump exchanges 3 intracellular Na + ions with 2 extracellular K + ions through coupling with ATP hydrolysis. One third of the ATP synthesized daily by an individual is spent to power the sodium-potassium pump. The molecular weight of the sodium-potassium pump is 237212.36 Da and its isoelectric point (pI) is 5.40. Cardiac glycosides such as ouabain can inhibit the sodium-potassium pump’s ability to transport ions effectively and are used in the therapeutic treatment of congestive heart failure (5). The sodium-potassium pump is a P-type ATPase sharing similarities with other P-type ATPases, notably the calcium-ATPase in the sarcoplasmic reticulum and the hydrogen-potassium ATPase in gastric cells (2). This process results in the generation of electrochemical gradients essential to, but not limited to, creating action potentials (2). The sodium-potassium pump (3B8E) from Sus scrofa establishes concentration gradients of potassium and sodium across plasma membranes in animal cells by using energy gained from ATP hydrolysis (1). The Sodium-Potassium Pump: Always Pumped Up