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. 2021 Aug 23;13(8):1667. doi: 10.3390/v13081667

Figure 2.

Figure 2

(a) Superposition between the X-ray structure of ACE2 in complex with RBD and the best re-docked pose after docking simulations through the HADDOCK tool. (b) Right-hand images show zoomed-in context of the ACE221–43 peptide at the interface between ACE2 and RBD. (c) Linear sequence of a truncated portion (21 to 43 aa) of the ACE2 receptor. (d) Three-dimensional (3D) representation of the three representative clusters of ACE221–43, the first of which is the most populated. Key contacting elements inside (e) front view of the RBD-up/ACE221–43 conformation, and (f) side view of the RBD-up/ACE221–43. All amino acid residues involved in H-bonds (dark blue) and salt bridges (purple) are shown in stick representation.