8Y7X
Structure of HCoV-HKU1A spike in the functionally anchored-3up conformation with 3TMPRSS2
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 | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC |
| Chain | Residue | Details |
| x | VAL292-CYS297 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV |
| Chain | Residue | Details |
| x | ASP435-VAL446 |
| site_id | PS01209 |
| Number of Residues | 23 |
| Details | LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CInpsnw.CDgvsHCpgg.EDEnr...C |
| Chain | Residue | Details |
| x | CYS127-CYS149 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Charge relay system => ECO:0000250 |
| Chain | Residue | Details |
| x | CYS297 | |
| x | ILE346 | |
| y | CYS297 | |
| y | ILE346 | |
| z | CYS297 | |
| z | ILE346 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | ACT_SITE: Charge relay system |
| Chain | Residue | Details |
| x | GLY442 | |
| y | GLY442 | |
| z | GLY442 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | SITE: Cleavage => ECO:0000269|PubMed:11245484 |
| Chain | Residue | Details |
| x | ILE256 | |
| B | ASN355 | |
| B | ASN433 | |
| B | ASN454 | |
| B | ASN470 | |
| B | ASN564 | |
| B | ASN666 | |
| B | ASN686 | |
| B | ASN705 | |
| B | ASN726 | |
| B | ASN775 | |
| y | ILE256 | |
| B | ASN780 | |
| B | ASN797 | |
| B | ASN928 | |
| B | ASN1215 | |
| B | ASN1225 | |
| B | ASN1244 | |
| B | ASN1251 | |
| B | ASN1260 | |
| B | ASN1281 | |
| A | ASN19 | |
| z | ILE256 | |
| A | ASN29 | |
| A | ASN58 | |
| A | ASN114 | |
| A | ASN132 | |
| A | ASN171 | |
| A | ASN188 | |
| A | ASN192 | |
| A | ASN251 | |
| A | ASN355 | |
| A | ASN433 | |
| B | ASN114 | |
| A | ASN454 | |
| A | ASN470 | |
| A | ASN564 | |
| A | ASN666 | |
| A | ASN686 | |
| A | ASN705 | |
| A | ASN726 | |
| A | ASN775 | |
| A | ASN780 | |
| A | ASN797 | |
| B | ASN132 | |
| A | ASN928 | |
| A | ASN1215 | |
| A | ASN1225 | |
| A | ASN1244 | |
| A | ASN1251 | |
| A | ASN1260 | |
| A | ASN1281 | |
| C | ASN19 | |
| C | ASN29 | |
| C | ASN58 | |
| B | ASN171 | |
| C | ASN114 | |
| C | ASN132 | |
| C | ASN171 | |
| C | ASN188 | |
| C | ASN192 | |
| C | ASN251 | |
| C | ASN355 | |
| C | ASN433 | |
| C | ASN454 | |
| C | ASN470 | |
| B | ASN188 | |
| C | ASN564 | |
| C | ASN666 | |
| C | ASN686 | |
| C | ASN705 | |
| C | ASN726 | |
| C | ASN775 | |
| C | ASN780 | |
| C | ASN797 | |
| C | ASN928 | |
| C | ASN1215 | |
| B | ASN192 | |
| C | ASN1225 | |
| C | ASN1244 | |
| C | ASN1251 | |
| C | ASN1260 | |
| C | ASN1281 | |
| B | ASN251 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| x | ASN214 | |
| x | ASN250 | |
| y | ASN214 | |
| y | ASN250 | |
| z | ASN214 | |
| z | ASN250 |
