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![[Figure 1]](ni5021fig1mag.jpg)
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Figure 1
Mutational blueprint of the RBD–ACE2 interface. (a) Heatmap plotting changes in the predicted binding affinity of RBD wt to ACE2. The RBD binding interface was screened in silico (Rodrigues et al., 2019  ) for amino-acid substitutions leading to a predicted enhanced affinity for ACE2. The working template was obtained from the X-ray coordinates deposited in the Protein Data Bank under accession code 6m0j. Those mutations that increase the affinity for ACE2 have a positive value and are highlighted in blue, while those that decrease the affinity of RBD for ACE2 have a negative value and are shown in red. (b) Overall cartoon representation of the RBD wt–ACE2 crystal structure (left panel) with position 498 in RBD wt and the surrounding residues highlighted in yellow. The right panel shows a closer image of Gln498 in RBD wt. The dashed line represents a likely (3.4 Å) hydrogen bond between Gln498 of RBD wt and Gln42 of ACE2. |
![[Figure 1]](ni5021fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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