EC Number   |
Protein Variants |
Reference |
|---|
   3.4.17.23 | analysis |
receptor binding domain-ACE2 binding assay based on time-resolved FRET, which reliably monitors the interaction in a physiologically relevant and cellular context. The modular assay can monitor the impact of different cellular components, such as heparan sulfate, lipids, and membrane proteins on the receptor binding domain-ACE2 interaction and it can be extended to the full-length spike protein. The assay is high throughput compatible and can detect small-molecule competitive and allosteric modulators of the receptor binding domain-ACE2 interaction |
764432 |
| 3.4.17.23 | D206G |
deleterious missense variant |
762786 |
| 3.4.17.23 | D355N |
variant exhibits lower binding to SARS-CoV-2 S protein |
762786 |
| 3.4.17.23 | D38V |
variant exhibits lower binding to SARS-CoV-2 S protein |
762786 |
| 3.4.17.23 | D509Yr |
variant exhibits lower binding to SARS-CoV-2 S protein |
762786 |
| 3.4.17.23 | E23K |
the variant in the binding region increases disease susceptibility towards SARS-CoV-2 |
762786 |
| 3.4.17.23 | E329G |
variant shows a strong binding affinity with SARS-CoV-2 spike protein variants with very strong E329G-V483A, E329G-G476S, strong E329G-A419S, E329G-A348T and moderate E329G-S383C,E329G-F486L interaction |
765112 |
| 3.4.17.23 | E37K |
non-synonymous single nucleotide polymorphism |
765112 |
| 3.4.17.23 | E484K |
mutation forms high-affinity complexes (~40% more than wild-type) |
763365 |
| 3.4.17.23 | E484K/N501Y |
variant possesses both enhanced affinity and antibody resistance |
763365 |
