Crystallization (Comment) | Organism |
---|---|
structure of the SARS-CoV-2 chimeric receptor binding domain with human ACE2 complex. Residues Ser19, Gln24, Thr27, Phe28, His34, Glu35, Asp38, Tyr41, Gln42, Leu45, Tyr83, Asn330, Lys353, Gly354, Asp355, and Arg357 have a critical role in the binding regions. SARS-CoV has relatively similar interaction binding sites to SARS-CoV-2 except for Ser19, Leu45, Leu79, Gln325, Gly326, and Glu329 which are not involved in the interaction in SARS-CoV-2 | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
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chrysin | shows a strong affinity for the active site of ACE2, ACE2-inhibitor complexes display structural stability with suitable binding energies. The interaction of chrysin with Phe40, Asp350, and Gly352 on ACE2 can interfere with the binding of SARS-CoV-2 | Homo sapiens | |
luteolin | shows a strong affinity for the active site of ACE2, ACE2-inhibitor complexes display structural stability with suitable binding energies | Homo sapiens | |
pimozide | effectively binds to the ACE2 binding site for SARS-CoV-2 spike protein, does not show stability during molecular dynamics simulation | Homo sapiens | |
Ursodeoxycholic acid | effectively binds to the ACE2 binding site for SARS-CoV-2 spike protein, does not show stability during molecular dynamics simulation | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9BYF1 | - |
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