Literature summary for 3.4.17.23 extracted from

Barros, E.; Casalino, L.; Gaieb, Z.; Dommer, A.; Wang, Y.; Fallon, L.; Raguette, L.; Belfon, K.; Simmerling, C.; Amaro, R.
The flexibility of ACE2 in the context of SARS-CoV-2 infection (2021), Biophys. J., 120, 1072-1084 .

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9BYF1	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	five glycans in ACE2 are in close proximity to the receptor-binding domain (RBD). N90, and to a lesser extent N322, of ACE2 establish contacts with RBD. N53 can form a large number of contacts with the RBD residues, whereas the RBD glycan N343 makes very few contacts with ACE2's head protein residues or glycans. Structural basis for the negative effect of glycan of N90 on receptor-binding domain (RBD) binding. Glycan N53 is involved in ACE2 homodimer and ACE2-RBD heterodimer contacts	Homo sapiens

Subunits

Subunits	Comment	Organism
homodimer	-	Homo sapiens

Synonyms

Synonyms	Comment	Organism
ACE2	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	ACE2 is the dominant host receptor of SARS-CoV-2	Homo sapiens

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Release 2023.1 (January 2023)