8XVM
Structure of SARS-CoV-2 BA.2.86 spike glycoprotein in complex with ACE2 (3-up state)
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007165 | biological_process | signal transduction |
| A | 0016020 | cellular_component | membrane |
| A | 0019031 | cellular_component | viral envelope |
| A | 0019062 | biological_process | virion attachment to host cell |
| A | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| A | 0019081 | biological_process | viral translation |
| A | 0020002 | cellular_component | host cell plasma membrane |
| A | 0039587 | biological_process | suppression by virus of host tetherin activity |
| A | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| A | 0039660 | molecular_function | structural constituent of virion |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043655 | cellular_component | host extracellular space |
| A | 0044173 | cellular_component | host cell endoplasmic reticulum-Golgi intermediate compartment membrane |
| A | 0044228 | cellular_component | host cell surface |
| A | 0046598 | biological_process | positive regulation of viral entry into host cell |
| A | 0046718 | biological_process | symbiont entry into host cell |
| A | 0046789 | molecular_function | host cell surface receptor binding |
| A | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
| A | 0048018 | molecular_function | receptor ligand activity |
| A | 0052170 | biological_process | symbiont-mediated suppression of host innate immune response |
| A | 0055036 | cellular_component | virion membrane |
| A | 0061025 | biological_process | membrane fusion |
| A | 0075509 | biological_process | endocytosis involved in viral entry into host cell |
| A | 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 |
| D | THR371-GLN380 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402 |
| Chain | Residue | Details |
| D | GLU375 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| D | HIS505 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774 |
| Chain | Residue | Details |
| D | ARG169 | |
| D | TRP477 | |
| D | LYS481 | |
| A | LEU804 | |
| A | PRO1077 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| D | ARG273 | |
| D | HIS345 | |
| D | TYR515 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
| Chain | Residue | Details |
| D | HIS374 | |
| D | HIS378 | |
| D | GLU402 | |
| A | PHE346 | |
| A | SER619 | |
| A | CYS660 | |
| A | PHE1101 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| D | ASN53 | |
| D | ASN322 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337 |
| Chain | Residue | Details |
| D | ASN90 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
| Chain | Residue | Details |
| D | ASN103 | |
| D | ASN432 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337 |
| Chain | Residue | Details |
| D | ASN546 |
| 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 |
| A | ARG679 | |
| A | SER681 |
| 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 |
| A | ASP1137 |
| 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 |
| A | ASP1161 | |
| A | ASN1176 |
