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. Author manuscript; available in PMC: 2021 Jun 14.
Published in final edited form as: Nat Struct Mol Biol. 2020 Jul 9;27(8):763–767. doi: 10.1038/s41594-020-0468-7

Figure 3. Binding of ACE2 receptor to bat virus and SARS-CoV-2 spike protein.

Figure 3

(A) Plot of surface biolayer amplitude measurement as a function of ACE2 concentration with the data for spike from SARS-CoV-2 (blue, Kd calculated as 91 ± 18 nM) and from the bat virus (red, Kd estimated to be >40 μM). The equilibrium dissociation constant for SARS-CoV-2 protein calculated from kinetic constants (koff = 0.0105 s-1 and kon = 1.56 x 105 M-1s-1) was 67.5 +/- 9 nM. (B & C) Ribbon representation of modelled molecular interactions between ACE2 (green) with RBD from spike in SARS-CoV-2 (blue) (both PDB 6VW121) and bat virus (brown, this study). (B) Details of a hydrophobic pocket on ACE2 that accommodates a phenylalanine residue from the SARS-CoV-2 S RBD. (C) Shows two salt bridges and a charged hydrogen bond linking SARS-CoV-2 S RBD to ACE2, while the interface with bat virus S RBD is not able to make these interactions and presents a potential steric clash between SARS-CoV-2 RBD Tyr493 with ACE2 Lys31.