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. 2020 Feb 28;10:3731. doi: 10.1038/s41598-020-60617-y

Figure 5.

Figure 5

AdiC N22A and L123W (3L1L) structure in outward-open occluded (OOO) state bound to Arginine. (a) Zoom on the top view of the OOO conformation bound to the substrate. Key contacts are observed between the backbone atoms of the conserved residues of TM1 (yellow) and TM6 (raspberry pink) and the amino acid moiety of the substrate. The side chain of the Arginine substrate is sandwiched between Trp202 (TM6) and Trp293 (TM8) and the guanidinium makes several H-bonds with the backbone of TM3 residues. (b) 2D diagram of interactions between the AdiC OOO structure and Arginine.