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. Author manuscript; available in PMC: 2023 Jul 22.
Published in final edited form as: ACS Synth Biol. 2021 Sep 1;10(9):2359–2370. doi: 10.1021/acssynbio.1c00258

Figure 2.

Figure 2.

Homology model of CHMO DTNP. (A) Overview of the cofactor binding pocket, NADH (in green) is pressed on one end by the control loop (pink). FAD (yellow) is held opposite of the NADH, and positions of the selected mutations are represented as spheres. (B) K349N supports the loop that S208D sits on, and S208D makes a bidentate hydrogen bond to the NADH adenosine ribose. (C) K326T initiates a hydrogen bond to the control loop at the backbone carbonyl of A487. The additional hydrogen bond may cause the control loop to favor maintaining the catalytically relevant, closed conformation. (D) L143P impacts the conformations that FAD can adopt.