8DMA
Cryo-EM structure of SARS-CoV-2 Omicron BA.1 spike protein in complex with mouse ACE2 (focused refinement of RBD and ACE2)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
| A | 0019031 | cellular_component | viral envelope |
| A | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| A | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| A | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
| A | 0055036 | cellular_component | virion membrane |
| A | 0075509 | biological_process | endocytosis involved in viral entry into host cell |
| D | 0006508 | biological_process | proteolysis |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| D | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355 |
| Chain | Residue | Details |
| D | GLU375 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355 |
| Chain | Residue | Details |
| D | HIS505 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355 |
| Chain | Residue | Details |
| D | ARG169 | |
| D | HIS374 | |
| D | HIS378 | |
| D | GLU402 | |
| D | TRP477 | |
| D | LYS481 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9BYF1 |
| Chain | Residue | Details |
| D | ARG273 | |
| D | HIS345 | |
| D | TYR515 | |
| A | ASN801 | |
| A | ASN1074 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| D | ASN53 | |
| D | ASN536 | |
| D | ASN546 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 7 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
| Chain | Residue | Details |
| A | TYR168 | |
| A | ASN282 | |
| A | ASN331 | |
| A | ASN343 | |
| A | ASN616 | |
| A | ASN657 | |
| A | ASN1098 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
| Chain | Residue | Details |
| A | ASN234 | |
| A | ASN709 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391 |
| Chain | Residue | Details |
| A | THR323 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391 |
| Chain | Residue | Details |
| A | SER325 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
| Chain | Residue | Details |
| A | ASN603 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583 |
| Chain | Residue | Details |
| A | THR676 | |
| A | THR678 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
| Chain | Residue | Details |
| A | ASN1134 |
