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Part-IAim of Present WorkFigure 1. Membrane domain of the H + /K + -ATPase E2-P model with pantoprazole, boundat Cys813 and Cys822 (stick with Connolly surfaces in cloud). A known site of a subunitinteraction (36, 37), S [910] YGQ, is highlighted (white ribbon) in the TM7/TM8 loop.Cys813, Cys892, and Cys321 are labeled (38) by various proton pump inhibitors (all atCys813, Omeprazole at Cys892, and lansoprazole at Cys321) and are solvent-accessiblein the model. Labeling at the latter two sites is not correlated with inhibition (3). Thecrossover point (“pivot”) between TM5 near Ile793 and TM7 near Gly867 (gold sphere)is apparently conserved in the P2-type ATPases. An extensive array of aromatic sidechains (in stick form) replaces non-aromatic Ca 2+ -ATPase residues and affects thespacing between helices. TM9 and TM10 are omitted for clarity. 5The entire cascade for the formation of disulfide is initiated by donation of an electronpair from the basic pyridinyl ‘N’ atom to the electron deficient ‘C’ of benzimidazole(Figure 2).57