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(A) The active sites in the dimer are interconnected through a π-stacking interactions and hydrogen bonds. One active site is in the open conformation and the other is closed as shown by the different Pro192 to NADP distances. NADP is shown as a spacefilling model. (B) Diagram of residues involved in the pathway that is proposed to allow communication between the active sites, with the bound inhibitor SMCS shown in lighter shading.
