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. Author manuscript; available in PMC: 2021 Nov 3.
Published in final edited form as: J Med Chem. 2021 May 4;64(9):5874–5885. doi: 10.1021/acs.jmedchem.1c00038

Figure 5.

Figure 5.

Molecular docking of heMAMP binding to MPO. (a) An intramolecular hydrogen bond formed between the two amide bonds increases the rigidity of heMAMP. (b) Representations of heMAMP (left) and MPO-Gd (right) binding to the MPO–CN complex using PyMol. Amino acid residues Q91, H95, and R239 (shown as lines) together with heme (in green sticks) form the active site of MPO. All of the other amino acid residues (as lines) shown are within 4 Å to heMAMP and MPO-Gd. The hydrogen bonds are shown as red dashes and the electrostatic interaction is shown as orange dashes.