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. 2019 Aug 7;294(40):14482–14498. doi: 10.1074/jbc.RA119.009214

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© 2019 Lang et al.

Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 5. — Interactions between GfTNMT and the N-methylated product SMS. Residues within 4 Å of SMS are shown as lines and presented in all-atom representation. Hydrogen bonds are represented as yellow-dashed lines. A, SMS is held in a bent conformation within the binding-site pocket through hydrophobic interactions between the protein and the protoberberine backbone of SMS. B, presence of a hydrogen bond network between two water molecules and O-16 helps to recognize the terminal methylenedioxy bridge adjacent to ring A of the isoquinoline portion of the BIA substrate.