Fig. 3: Interface comparison among ACE2 orthologs binding with RaTG13-RBD, SARS-COV-2 PT-RBD, SARS-CoV-RBD and Omicron BA.1-RBD. | Nature Communications

Fig. 3: Interface comparison among ACE2 orthologs binding with RaTG13-RBD, SARS-COV-2 PT-RBD, SARS-CoV-RBD and Omicron BA.1-RBD.

From: Binding and structural basis of equine ACE2 to RBDs from SARS-CoV, SARS-CoV-2 and related coronaviruses

Fig. 3

a–d Binding interface of eq (a, left) and hACE2 (a, right) with the RaTG13-RBD (b), and the corresponding interface of eq and hACE2 binding to the SARS-COV-2 PT-RBD (c, d). e–g Interface difference of the RBDs between the eqACE2/RaTG13-RBD and eqACE2/SARS-COV-2 PT-RBD complexes (e), ACE2s between the eqACE2/SARS-COV-2 PT-RBD and hACE2/SARS-COV-2 PT-RBD complexes (f), and ACE2s between the eqACE2/RaTG13-RBD and hACE2/RaTG13-RBD complexes (g). h Binding sites of hACE2 (up, light blue) and its corresponding residues in eqACE2 (purple, down). Particularly, substitutions of referred residues are labelled in yellow. i, j The binding interface of eqACE2/Omicron BA.1-RBD (i) and hACE2/Omicron BA.1-RBD (j) are shown and the interacting residues are labeled. k The distinctive interacting residues of RBDs between eqACE2/Omicron BA.1-RBD and eqACE2/SARS-COV-2 PT-RBD.

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