8XV0
Structure of SARS-CoV-2 BA.2.86 spike RBD in complex with ACE2 (up state)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007165 | biological_process | signal transduction |
| B | 0016020 | cellular_component | membrane |
| B | 0019031 | cellular_component | viral envelope |
| B | 0019062 | biological_process | virion attachment to host cell |
| B | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| B | 0019081 | biological_process | viral translation |
| B | 0020002 | cellular_component | host cell plasma membrane |
| B | 0039587 | biological_process | suppression by virus of host tetherin activity |
| B | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| B | 0039660 | molecular_function | structural constituent of virion |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043655 | cellular_component | host extracellular space |
| B | 0044173 | cellular_component | host cell endoplasmic reticulum-Golgi intermediate compartment membrane |
| B | 0044228 | cellular_component | host cell surface |
| B | 0046598 | biological_process | positive regulation of viral entry into host cell |
| B | 0046718 | biological_process | symbiont entry into host cell |
| B | 0046789 | molecular_function | host cell surface receptor binding |
| B | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
| B | 0048018 | molecular_function | receptor ligand activity |
| B | 0052170 | biological_process | symbiont-mediated suppression of host innate immune response |
| B | 0055036 | cellular_component | virion membrane |
| B | 0061025 | biological_process | membrane fusion |
| B | 0075509 | biological_process | endocytosis involved in viral entry into host cell |
| B | 0098670 | biological_process | entry receptor-mediated virion attachment to host cell |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ |
| Chain | Residue | Details |
| A | THR371-GLN380 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | SITE: Cleavage; by host furin => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32362314, ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616 |
| Chain | Residue | Details |
| B | GLN689 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | SITE: Cleavage; by host TMPRSS2 or CTSL => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616 |
| Chain | Residue | Details |
| B | ASP819 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | CARBOHYD: N-linked (GlcNAc...) (hybrid) 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 |
| B | ASN65 | |
| B | THR126 | |
| B | VAL721 | |
| B | LEU805 | |
| B | PRO1078 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
| Chain | Residue | Details |
| B | THR78 | |
| B | TRP153 | |
| B | ASP1198 |
| site_id | SWS_FT_FI5 |
| 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 |
| B | PHE169 | |
| B | THR286 | |
| B | LEU335 | |
| B | PHE347 | |
| B | SER620 | |
| B | CYS661 | |
| B | PHE1102 |
| site_id | SWS_FT_FI6 |
| 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 |
| B | PHE238 | |
| B | ILE713 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391 |
| Chain | Residue | Details |
| B | VAL327 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391 |
| Chain | Residue | Details |
| B | PHE329 | |
| A | ASN432 |
| site_id | SWS_FT_FI9 |
| 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 |
| B | VAL607 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583 |
| Chain | Residue | Details |
| B | ARG680 | |
| B | SER682 |
| site_id | SWS_FT_FI11 |
| 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 |
| B | ASP1138 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
| Chain | Residue | Details |
| B | ASP1162 | |
| B | ASN1177 |
