7WPC
The second RBD of SARS-CoV-2 Omicron Variant in complexed with RBD-ACE2
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 |
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 | 722 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
B | SER682 | |
D | GLN18-SER740 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | TRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU01354 |
Chain | Residue | Details |
B | ARG812 | |
D | ILE741-ILE761 |
site_id | SWS_FT_FI3 |
Number of Residues | 43 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
B | ASN17 | |
A | ASN1155 | |
A | ASN1170 | |
B | ASN1155 | |
B | ASN1170 | |
D | PHE762-PHE805 |
site_id | SWS_FT_FI4 |
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 |
A | THR122 | |
B | ASN61 | |
B | THR122 | |
B | ASN1071 | |
A | ASN714 | |
A | ASN798 | |
A | ASN1071 | |
B | ASN714 | |
B | ASN798 | |
D | GLU375 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
A | GLU149 | |
B | THR74 | |
B | GLU149 | |
A | ASN1191 | |
B | ASN1191 | |
D | HIS505 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774 |
Chain | Residue | Details |
D | LYS481 | |
B | TYR165 | |
B | ASN328 | |
B | ASN340 | |
B | ASN613 | |
B | ASN654 | |
B | ASN1095 | |
A | ASN340 | |
A | ASN613 | |
A | ASN654 | |
A | ASN1095 | |
B | ASN279 | |
D | TRP477 | |
D | ARG169 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
B | ASN706 | |
D | ARG273 | |
D | TYR515 | |
D | HIS345 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
D | HIS374 | |
D | GLU402 | |
D | HIS378 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498 |
Chain | Residue | Details |
B | SER322 | |
D | TYR781 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498 |
Chain | Residue | Details |
B | ASN600 | |
D | SER783 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
B | THR673 | |
B | THR675 | |
D | ASN322 | |
D | ASN53 |
site_id | SWS_FT_FI12 |
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 | ASN1131 | |
D | ASN90 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
D | ASN103 | |
D | ASN432 |
site_id | SWS_FT_FI14 |
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 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
D | ASN690 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36876523 |
Chain | Residue | Details |
D | LYS788 |