Figure 2 (A) Rhinolophus ferrumequinum and Myotis daubentonii ACE2 in complex with SARS-CoV-2 S RBD. The structures are superimposed to hACE2 structure in complex with SARS-CoV-2 S RBD. The data, extracted from the last step of molecular dynamics, are relative to 1–358 ACE2 residues. (B) Multiple sequence alignment including hACE2 and ACE2 of Rhinolophus ferrumequinum and Myotis daubentonii. Residues involved in the interaction with S protein are shown: the residue numbers in red represent the residues essential for hACE2/SARS-CoV-2 S binding. Conserved residues are highlighted in blue, while similar residues are highlighted in green. Bold black residue numbers indicate amino acids essential for the stability of hACE2/SARS-CoV-2 S interaction.