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. 2022 Jul 22;9:846996. doi: 10.3389/fmolb.2022.846996

FIGURE 2.

FIGURE 2

Sustained interaction of S1-RBD Y501 residue (N501Y mutant) with ACE2. (A) Temporal evolution of residues Y41 and K353 in ACE2 and either the N501 in the WT S1-RBD (left panel) or the Y501 in the N501Y mutant S1-RBD (right panel) in the MD simulation. A total of 11 frames obtained from up to 100 s simulations, each 10 ns apart, were compiled together. Note the increased fluctuation of the N501 residue in the WT S1-RBD. (B–E) Graph showing inter-residue distances between the center of masses of residue Y41 in ACE2 and N501 in the WT and Y501 in the N501Y mutant S1-RBD (B), K353 in ACE2 and N501 in the WT and Y501 in the N501Y mutant S1-RBD (C), Q24 in ACE2 and N487 in either the WT or the N501Y mutant S1-RBD (D), and T27 in ACE2 and Y489 in either the WT or the N501Y mutant S1-RBD (E). Note the increased inter-residue distance fluctuations between the residues Y41 and K353 in ACE2 and N501 in S1-RBD in the WT ACE2-S1-RBD complex compared to the N501Y mutant complex (B,C).