8WRM
XBB.1.5 spike protein in complex with ACE2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| F | 0016020 | cellular_component | membrane |
| F | 0019031 | cellular_component | viral envelope |
| F | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| F | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| F | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
| F | 0055036 | cellular_component | virion membrane |
| F | 0075509 | biological_process | endocytosis involved in viral entry into host cell |
| G | 0016020 | cellular_component | membrane |
| G | 0019031 | cellular_component | viral envelope |
| G | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| G | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| G | 0046813 | biological_process | receptor-mediated virion attachment to host cell |
| G | 0055036 | cellular_component | virion membrane |
| G | 0075509 | biological_process | endocytosis involved in viral entry into host cell |
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 | |
| G | ARG685 | |
| C | ARG685 |
| 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 | |
| G | ARG815 | |
| C | ARG815 |
| 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 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| D | ARG273 | |
| G | ASN1074 | |
| C | ASN61 | |
| C | ASN122 | |
| C | ASN717 | |
| C | ASN801 | |
| C | ASN1074 | |
| D | HIS345 | |
| D | TYR515 | |
| F | ASN801 | |
| F | ASN1074 | |
| G | ASN61 | |
| G | ASN122 | |
| G | ASN717 | |
| G | ASN801 |
| 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 | |
| G | ASN149 | |
| C | ASN74 | |
| C | ASN149 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| D | ASN53 | |
| G | ASN331 | |
| G | ASN343 | |
| G | ASN616 | |
| G | ASN657 | |
| G | ASN1098 | |
| C | ASN165 | |
| C | ASN282 | |
| C | ASN331 | |
| C | ASN343 | |
| C | ASN616 | |
| D | ASN322 | |
| C | ASN657 | |
| C | ASN1098 | |
| F | ASN331 | |
| F | ASN343 | |
| F | ASN616 | |
| F | ASN657 | |
| F | ASN1098 | |
| G | ASN165 | |
| G | ASN282 |
| 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 | |
| F | ASN709 | |
| G | ASN234 | |
| G | ASN709 | |
| C | ASN234 | |
| C | ASN709 |
| 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 | THR323 |
| 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 | |
| G | SER325 | |
| C | SER325 |
| 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 |
| F | ASN603 | |
| G | ASN603 | |
| C | ASN603 |
| 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 |
| F | THR676 | |
| F | THR678 | |
| G | THR676 | |
| G | THR678 | |
| C | THR676 | |
| C | THR678 |
| 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 |
| F | ASN1134 | |
| G | ASN1134 | |
| C | ASN1134 |
