9ASD
VIR-7229 Fab fragment bound the SARS-CoV-2 BA.2.86 spike trimer (local refinement of the BA 2.86 RBD/VIR-7229 VHVL)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| H | 0002250 | biological_process | adaptive immune response |
| H | 0002376 | biological_process | immune system process |
| H | 0005576 | cellular_component | extracellular region |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0016020 | cellular_component | membrane |
| H | 0019814 | cellular_component | immunoglobulin complex |
| R | 0005515 | molecular_function | protein binding |
| R | 0005886 | cellular_component | plasma membrane |
| R | 0007165 | biological_process | signal transduction |
| R | 0016020 | cellular_component | membrane |
| R | 0019031 | cellular_component | viral envelope |
| R | 0019062 | biological_process | virion attachment to host cell |
| R | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| R | 0019081 | biological_process | viral translation |
| R | 0020002 | cellular_component | host cell plasma membrane |
| R | 0033644 | cellular_component | host cell membrane |
| R | 0039587 | biological_process | symbiont-mediated-mediated suppression of host tetherin activity |
| R | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| R | 0039660 | molecular_function | structural constituent of virion |
| R | 0039663 | biological_process | membrane fusion involved in viral entry into host cell |
| R | 0042802 | molecular_function | identical protein binding |
| R | 0043655 | cellular_component | host extracellular space |
| R | 0044173 | cellular_component | host cell endoplasmic reticulum-Golgi intermediate compartment membrane |
| R | 0044228 | cellular_component | host cell surface |
| R | 0044423 | cellular_component | virion component |
| R | 0046598 | biological_process | positive regulation of viral entry into host cell |
| R | 0046718 | biological_process | symbiont entry into host cell |
| R | 0046789 | molecular_function | host cell surface receptor binding |
| R | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
| R | 0048018 | molecular_function | receptor ligand activity |
| R | 0052170 | biological_process | symbiont-mediated suppression of host innate immune response |
| R | 0055036 | cellular_component | virion membrane |
| R | 0061025 | biological_process | membrane fusion |
| R | 0075509 | biological_process | endocytosis involved in viral entry into host cell |
| R | 0098670 | biological_process | entry receptor-mediated virion attachment to host cell |
| R | 0141146 | biological_process | symbiont-mediated disruption of host tissue |
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 |
| R | GLN690 |
| 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 |
| R | ASP820 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| 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 |
| R | PRO21 | |
| R | ASP1163 | |
| R | ASN1178 |
| site_id | SWS_FT_FI4 |
| 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 |
| R | ASN65 | |
| R | THR126 | |
| R | VAL722 | |
| R | LEU806 | |
| R | PRO1079 |
| site_id | SWS_FT_FI5 |
| 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 |
| R | THR78 | |
| R | TRP153 | |
| R | ASP1199 |
| 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 |
| R | PHE169 | |
| R | THR286 | |
| R | LEU335 | |
| R | PHE347 | |
| R | SER621 | |
| R | CYS662 | |
| R | PHE1103 |
| 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 |
| R | PHE238 | |
| R | ILE714 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391 |
| Chain | Residue | Details |
| R | VAL327 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391 |
| Chain | Residue | Details |
| R | PHE329 |
| 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 |
| R | VAL608 |
| 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 |
| R | ARG681 | |
| R | SER683 |
| 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 |
| R | ASP1139 |
