Fig. 1

Alignment and electrostatic surface potential analysis of key amino acids residues of ACE2. A Sequence alignment analysis of the interface binding between ACE2 and S of SARS-CoV-2 from minks (GenBank accession no. XP_044091953.1), ferrets (GenBank accession no. NP_001297119.1), rhesus monkeys (GenBank accession no. NP_001129168.1), humans (GenBank accession no. NP_001358344.1), mice (GenBank accession no. NP_001123985.1), hamsters (GenBank accession no. XP_003503283.1) and bovines (GenBank accession no. NP_001019673.2). The ACE2 residues at positions 342, 368, 386, 502, and 507 are marked with blue triangles. B Electrostatic surface potential diagram of ACE2s in different species. The structural superposition of the ACE2 region 341–480 from cattle (green), minks (brown), ferrets (cyan), mice (gray), hamsters (pink), humans (khaki), and rhesus monkeys (blue) is in the center. The homology models of human ACE2 (PDBID 6m18) were used to compare the ACE2 structures of cattle, minks, ferrets, mice, hamsters, and rhesus monkeys. The tertiary structure was predicted using SWISS-MODEL. The yellow sticks highlight the five key differential residues of ACE2 binding with S of SARS-CoV-2. The details are circled using a dashed line in each electrostatic surface potential map. The electrostatic potential color range is –/ + 5