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. 2018 Jun 28;57(33):10600–10604. doi: 10.1002/anie.201805060

Figure 2.

Figure 2

(A) The structure of CNMT (PDB 6GKV) with AdoHcy in red and the product N‐methylheliamine 8 a in green (ball and stick) showing key amino acid residues involved in catalysis or substrate recognition. (B) mFo‐mFc electron density maps (contoured at 3.5 σ) of AdoHcy and 8 a in the CNMT active site. Structure of substrate heliamine 8, N‐methylated product 8 a and substrate analog 9. (C) Model of the CNMT (R)‐coclaurine 4 docked in the active site and (D) a model derived from docking (S)‐4. (E) Proposed mechanism of CNMT showing the putative role of key active site amino acid residues.