8XLM
Structure of the SARS-CoV-2 EG.5.1 spike glycoprotein in complex with ACE2 (1-up state)
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 |
| D | 0006508 | biological_process | proteolysis |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| D | 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 |
| 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 | |
| B | SER689 | |
| C | SER689 |
| 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 | |
| B | GLU819 | |
| C | GLU819 |
| 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 | |
| B | ASN20 | |
| B | PRO1162 | |
| B | VAL1177 | |
| C | ASN20 | |
| C | PRO1162 | |
| C | VAL1177 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| D | ARG273 | |
| B | ALA1078 | |
| C | TRP64 | |
| C | ASN125 | |
| C | SER721 | |
| C | ILE805 | |
| C | ALA1078 | |
| D | HIS345 | |
| D | TYR515 | |
| A | ILE805 | |
| A | ALA1078 | |
| B | TRP64 | |
| B | ASN125 | |
| B | SER721 | |
| B | ILE805 |
| 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 | |
| B | LYS77 | |
| B | MET153 | |
| B | ILE1198 | |
| C | LYS77 | |
| C | MET153 | |
| C | ILE1198 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| D | ASN53 | |
| B | LEU335 | |
| B | PHE347 | |
| B | VAL620 | |
| B | GLU661 | |
| B | TRP1102 | |
| C | GLU169 | |
| C | THR286 | |
| C | LEU335 | |
| C | PHE347 | |
| C | VAL620 | |
| D | ASN322 | |
| C | GLU661 | |
| C | TRP1102 | |
| A | LEU335 | |
| A | PHE347 | |
| A | VAL620 | |
| A | GLU661 | |
| A | TRP1102 | |
| B | GLU169 | |
| B | THR286 |
| 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 | |
| A | ALA713 | |
| B | PHE238 | |
| B | ALA713 | |
| C | PHE238 | |
| C | ALA713 |
| 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 | |
| C | VAL327 |
| 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 | |
| B | PHE329 | |
| C | PHE329 |
| 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 | GLN607 | |
| B | GLN607 | |
| C | GLN607 |
| 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 | SER680 | |
| A | GLY682 | |
| B | SER680 | |
| B | GLY682 | |
| C | SER680 | |
| C | GLY682 |
| 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 | TYR1138 | |
| B | TYR1138 | |
| C | TYR1138 |
