"b,c, Ribbon representation of modeled molecular interactions between ACE2 (green) with RBD from S in SARS-CoV-2 (blue) (both PDB 6VW1)21 and bat virus (red, this study). 
b, Details of a hydrophobic pocket on ACE2 that accommodates a phenylalanine residue from the SARS-CoV-2 S RBD. 
c, 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 Tyr493 and ACE2 Lys31."

University of Michigan - Ann Arbor

Differences in potential binding interactions were found between ACE2 domain and RBD domain of SARS-CoV-2 and RaTG13 S trimers. SARS-CoV-2 has Phe486 interacting with ACE2 human receptor while the bat virus has Leu486 instead, which is less bulky. SARS-CoV-2 also has a Gln493 that is able to form a hydrogen bond of Glu35 in ACE2, while RaTG13 has a tyrosine that is unlikely to bond with Glu35. More differences are shown in Fig 3b and Fig 3c. These distinctions may impact the differences in S glycoprotein affinity to ACE2 between SARS-CoV-2 and RaTG13. 

Differences in potential binding interactions between ACE2 domain and RBD domain of SARS-CoV-2 and RaTG13 S glycoprotein

Wrobel, A.G., Benton, D.J., Xu, P. et al. SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects. Nat Struct Mol Biol (2020). https://doi.org/10.1038/s41594-020-0468-7

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