This PDF file includes:

• Fig. S1. Electron density maps of ligands in the TmPPase:IDP:ATC structure.
• Fig. S2. Asymmetric unit of TmPPase:IDP:ATC.
• Fig. S3. Oligomerization state of TmPPase upon the addition of inhibitors.
• Fig. S4. Comparison of the ATC binding sites in different TmPPase structures.
• Fig. S5. Differences in the ATC binding site between monomers of the TmPPase:IDP:ATC structure.
• Fig. S6. Effect of ATC on growth of P. falciparum and on PfPPase.
• Fig. S7. Linearity of TmPPase activity as a function of time and concentration.
• Fig. S8. Multiple sequence alignment of mPPases from different organisms.
• Scheme S1. Synthesis of analogs of 1 with heavy and basic atoms.
• Table S1. X-ray data collection and refinement statistics.
• Table S2. RMSD of TmPPase monomer in the asymmetric unit relative to monomer A.
• Table S3. Major interactions of ATC with chains A and D.
• Table S4. RMSD between chains A and B of loops in different TmPPase structures.
• Table S5. RMSD of chain A of TmPPase:IDP:ATC loops to chain A of TmPPase:IDP loops.
• Table S6. Hill constant of TmPPase inhibition by ATC at different substrate concentrations.
• References (56–58)

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