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. 2020 Oct 13;21(20):7562. doi: 10.3390/ijms21207562

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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DM-ActKR monomer conformation comparison and two major binding motif clusters generated from docking analysis on octaketide-bound DM-ActKR monomer (closed conformation). (A) Visualization of aligned monomers among the structures originally containing: octaketide-bound (gold), tetraketide-bound (cyan), and no ligand (pink). The NADPH present in all three structures is displayed; ligands deleted for clarity. (B) The front-patch binding motif. (C) The back-patch binding motif. The protein and NADPH surface are displayed in gold.