7XO7
SARS-CoV-2 Omicron BA.2 Variant Spike Trimer with two human ACE2 Bound
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 |
E | 0006508 | biological_process | proteolysis |
E | 0008237 | molecular_function | metallopeptidase activity |
E | 0008241 | molecular_function | peptidyl-dipeptidase activity |
E | 0016020 | cellular_component | membrane |
F | 0006508 | biological_process | proteolysis |
F | 0008237 | molecular_function | metallopeptidase activity |
F | 0008241 | molecular_function | peptidyl-dipeptidase activity |
F | 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 |
E | THR371-GLN380 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1444 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
E | GLN18-SER740 | |
F | GLN18-SER740 | |
C | GLN17-ILE1216 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | TRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU01354 |
Chain | Residue | Details |
E | ILE741-ILE761 | |
F | ILE741-ILE761 | |
C | TRP1217-MET1237 |
site_id | SWS_FT_FI3 |
Number of Residues | 86 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
E | PHE762-PHE805 | |
F | PHE762-PHE805 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402 |
Chain | Residue | Details |
E | GLU375 | |
F | GLU375 | |
C | ALA688 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
E | HIS505 | |
F | HIS505 | |
C | ILE818 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774 |
Chain | Residue | Details |
E | ARG169 | |
B | GLY1246 | |
C | THR1238 | |
C | SER1239 | |
C | CYS1243 | |
C | LEU1244 | |
C | GLY1246 | |
E | TRP477 | |
E | LYS481 | |
F | ARG169 | |
F | TRP477 | |
F | LYS481 | |
B | SER1239 | |
B | CYS1243 | |
B | LEU1244 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
E | ARG273 | |
B | ASP1257 | |
C | CYS1250 | |
C | GLY1251 | |
C | CYS1253 | |
C | PHE1256 | |
C | ASP1257 | |
E | HIS345 | |
E | TYR515 | |
F | ARG273 | |
F | HIS345 | |
F | TYR515 | |
B | GLY1251 | |
B | CYS1253 | |
B | PHE1256 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
E | HIS374 | |
E | HIS378 | |
E | GLU402 | |
F | HIS374 | |
F | HIS378 | |
F | GLU402 | |
C | ASN20 | |
C | SER1161 | |
C | VAL1176 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498 |
Chain | Residue | Details |
E | TYR781 | |
B | THR1077 | |
C | TRP64 | |
C | ASN125 | |
C | ILE720 | |
C | GLN804 | |
C | THR1077 | |
F | TYR781 | |
A | ILE720 | |
A | GLN804 | |
A | THR1077 | |
B | TRP64 | |
B | ASN125 | |
B | ILE720 | |
B | GLN804 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498 |
Chain | Residue | Details |
E | SER783 | |
F | SER783 | |
A | LEU1197 | |
B | LYS77 | |
B | TRP152 | |
B | LEU1197 | |
C | LYS77 | |
C | TRP152 | |
C | LEU1197 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
E | ASN53 | |
B | ASN334 | |
B | ARG346 | |
B | GLU619 | |
B | TYR660 | |
B | HIS1101 | |
C | PHE168 | |
C | ILE285 | |
C | ASN334 | |
C | ARG346 | |
C | GLU619 | |
E | ASN322 | |
C | TYR660 | |
C | HIS1101 | |
F | ASN53 | |
F | ASN322 | |
A | GLU619 | |
A | TYR660 | |
A | HIS1101 | |
B | PHE168 | |
B | ILE285 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337 |
Chain | Residue | Details |
E | ASN90 | |
F | ASN90 | |
B | ARG237 | |
B | ILE712 | |
C | ARG237 | |
C | ILE712 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
E | ASN103 | |
E | ASN432 | |
F | ASN103 | |
F | ASN432 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337 |
Chain | Residue | Details |
E | ASN546 | |
F | ASN546 | |
C | ARG328 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
E | ASN690 | |
F | ASN690 | |
C | ASN606 |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36876523 |
Chain | Residue | Details |
E | LYS788 | |
A | HIS681 | |
F | LYS788 | |
B | HIS681 | |
C | LYS679 | |
C | HIS681 |
site_id | SWS_FT_FI17 |
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 |