8YZD
Structure of JN.1 RBD protein in complex with ACE2.
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 | 0033644 | cellular_component | host cell membrane |
A | 0039587 | biological_process | symbiont-mediated-mediated suppression 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 | 0039663 | biological_process | membrane fusion involved in viral entry into host cell |
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 | 0044423 | cellular_component | virion component |
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 |
A | 0141146 | biological_process | symbiont-mediated disruption of host tissue |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008241 | molecular_function | peptidyl-dipeptidase activity |
B | 0016020 | cellular_component | membrane |
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 |
B | 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 |
B | 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 |
B | 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 |
B | ARG169 | |
B | TRP477 | |
B | LYS481 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
B | ARG273 | |
B | HIS345 | |
B | TYR515 | |
A | PRO809 | |
A | CYS1082 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
B | HIS374 | |
B | HIS378 | |
B | GLU402 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
B | ASN53 | |
B | ASN322 | |
A | PHE338 | |
A | VAL350 | |
A | ILE624 | |
A | PRO665 | |
A | GLN1106 |
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 |
B | ASN90 | |
A | ASN717 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
B | ASN103 | |
B | 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 |
B | ASN546 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN690 |
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 | ALA684 | |
A | SER686 |
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 | GLN1142 |