8DM3
Cryo-EM structure of SARS-CoV-2 Omicron BA.2 spike protein in complex with Fab 4A8
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 |
B | 0016020 | cellular_component | membrane |
B | 0019031 | cellular_component | viral envelope |
B | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
B | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
B | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
B | 0055036 | cellular_component | virion membrane |
B | 0075509 | biological_process | endocytosis involved in viral entry into host cell |
C | 0016020 | cellular_component | membrane |
C | 0019031 | cellular_component | viral envelope |
C | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
C | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
C | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
C | 0055036 | cellular_component | virion membrane |
C | 0075509 | biological_process | endocytosis involved in viral entry into host cell |
Functional Information from PROSITE/UniProt
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH |
Chain | Residue | Details |
H | TYR228-HIS234 | |
L | TYR217-HIS223 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
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 |
A | ALA688 | |
B | ALA688 | |
C | ALA688 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
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 |
A | ILE818 | |
B | ILE818 | |
C | ILE818 |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
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 | ASN17 | |
A | SER1161 | |
A | VAL1176 | |
B | ASN17 | |
B | SER1161 | |
B | VAL1176 | |
C | ASN17 | |
C | SER1161 | |
C | VAL1176 |
site_id | SWS_FT_FI4 |
Number of Residues | 15 |
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 |
A | TRP64 | |
B | THR1077 | |
C | TRP64 | |
C | ASN125 | |
C | ILE720 | |
C | GLN804 | |
C | THR1077 | |
A | ASN125 | |
A | ILE720 | |
A | GLN804 | |
A | THR1077 | |
B | TRP64 | |
B | ASN125 | |
B | ILE720 | |
B | GLN804 |
site_id | SWS_FT_FI5 |
Number of Residues | 9 |
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 |
A | LYS77 | |
A | TRP152 | |
A | LEU1197 | |
B | LYS77 | |
B | TRP152 | |
B | LEU1197 | |
C | LYS77 | |
C | TRP152 | |
C | LEU1197 |
site_id | SWS_FT_FI6 |
Number of Residues | 21 |
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 | PHE168 | |
B | ASN334 | |
B | ARG346 | |
B | GLU619 | |
B | TYR660 | |
B | HIS1101 | |
C | PHE168 | |
C | ILE285 | |
C | ASN334 | |
C | ARG346 | |
C | GLU619 | |
A | ILE285 | |
C | TYR660 | |
C | HIS1101 | |
A | ASN334 | |
A | ARG346 | |
A | GLU619 | |
A | TYR660 | |
A | HIS1101 | |
B | PHE168 | |
B | ILE285 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
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 | ARG237 | |
A | ILE712 | |
B | ARG237 | |
B | ILE712 | |
C | ARG237 | |
C | ILE712 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | CARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391 |
Chain | Residue | Details |
A | ILE326 | |
B | ILE326 | |
C | ILE326 |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391 |
Chain | Residue | Details |
A | ARG328 | |
B | ARG328 | |
C | ARG328 |
site_id | SWS_FT_FI10 |
Number of Residues | 3 |
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 | ASN606 | |
B | ASN606 | |
C | ASN606 |
site_id | SWS_FT_FI11 |
Number of Residues | 6 |
Details | CARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583 |
Chain | Residue | Details |
A | LYS679 | |
A | HIS681 | |
B | LYS679 | |
B | HIS681 | |
C | LYS679 | |
C | HIS681 |
site_id | SWS_FT_FI12 |
Number of Residues | 3 |
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 | VAL1137 | |
B | VAL1137 | |
C | VAL1137 |