8WLZ
Cryo-EM structure of the WIV1 S-hACE2 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
| A | 0019031 | cellular_component | viral envelope |
| A | 0019062 | biological_process | virion attachment to host cell |
| A | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| A | 0020002 | cellular_component | host cell plasma membrane |
| A | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| A | 0044173 | cellular_component | host cell endoplasmic reticulum-Golgi intermediate compartment membrane |
| A | 0046718 | biological_process | symbiont entry into host cell |
| 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 | 0019062 | biological_process | virion attachment to host cell |
| B | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| B | 0020002 | cellular_component | host cell plasma membrane |
| B | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| B | 0044173 | cellular_component | host cell endoplasmic reticulum-Golgi intermediate compartment membrane |
| B | 0046718 | biological_process | symbiont entry into host cell |
| 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 | 0019062 | biological_process | virion attachment to host cell |
| C | 0019064 | biological_process | fusion of virus membrane with host plasma membrane |
| C | 0020002 | cellular_component | host cell plasma membrane |
| C | 0039654 | biological_process | fusion of virus membrane with host endosome membrane |
| C | 0044173 | cellular_component | host cell endoplasmic reticulum-Golgi intermediate compartment membrane |
| C | 0046718 | biological_process | symbiont entry into host cell |
| 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 | 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 | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402 |
| Chain | Residue | Details |
| D | GLU375 | |
| G | GLU375 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| D | HIS505 | |
| G | HIS505 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| 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 | |
| G | ARG169 | |
| G | TRP477 | |
| G | LYS481 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| D | ARG273 | |
| D | HIS345 | |
| D | TYR515 | |
| G | ARG273 | |
| G | HIS345 | |
| G | TYR515 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
| Chain | Residue | Details |
| D | HIS374 | |
| D | HIS378 | |
| D | GLU402 | |
| G | HIS374 | |
| G | HIS378 | |
| G | GLU402 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| D | ASN53 | |
| D | ASN322 | |
| G | ASN53 | |
| G | ASN322 |
| site_id | SWS_FT_FI7 |
| 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 |
| D | ASN90 | |
| G | ASN90 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
| Chain | Residue | Details |
| D | ASN103 | |
| D | ASN432 | |
| G | ASN103 | |
| G | ASN432 |
| site_id | SWS_FT_FI9 |
| 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 |
| D | ASN546 | |
| G | ASN546 |
