8XAL
Cryo-EM structure of SARS-CoV-2 S-BQ.1 in complex with 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 |
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 |
I | 0006091 | biological_process | generation of precursor metabolites and energy |
I | 0006508 | biological_process | proteolysis |
I | 0008218 | biological_process | bioluminescence |
I | 0008237 | molecular_function | metallopeptidase activity |
I | 0008241 | molecular_function | peptidyl-dipeptidase activity |
I | 0016020 | cellular_component | membrane |
J | 0006091 | biological_process | generation of precursor metabolites and energy |
J | 0006508 | biological_process | proteolysis |
J | 0008218 | biological_process | bioluminescence |
J | 0008237 | molecular_function | metallopeptidase activity |
J | 0008241 | molecular_function | peptidyl-dipeptidase activity |
J | 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 |
I | 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 |
I | GLU375 | |
J | GLU375 | |
C | GLN685 |
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 |
I | HIS505 | |
J | HIS505 | |
C | ASP815 |
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 |
I | ARG169 | |
I | TRP477 | |
I | LYS481 | |
J | ARG169 | |
J | TRP477 | |
J | LYS481 | |
C | ASN17 | |
C | ASP1158 | |
C | ASN1173 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
I | ARG273 | |
B | PRO1074 | |
C | TRP61 | |
C | VAL122 | |
C | VAL717 | |
C | LEU801 | |
C | PRO1074 | |
I | HIS345 | |
I | TYR515 | |
J | ARG273 | |
J | HIS345 | |
J | TYR515 | |
B | VAL122 | |
B | VAL717 | |
B | LEU801 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
I | HIS374 | |
I | HIS378 | |
I | GLU402 | |
J | HIS374 | |
J | HIS378 | |
J | GLU402 | |
C | PHE74 | |
C | GLU149 | |
C | ASP1194 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
I | ASN53 | |
B | CYS331 | |
B | ALA343 | |
B | PRO616 | |
B | CYS657 | |
B | PHE1098 | |
C | TYR165 | |
C | ASP282 | |
C | CYS331 | |
C | ALA343 | |
C | PRO616 | |
I | ASN322 | |
C | CYS657 | |
C | PHE1098 | |
J | ASN53 | |
J | ASN322 | |
A | PRO616 | |
A | CYS657 | |
A | PHE1098 | |
B | TYR165 | |
B | ASP282 |
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 |
I | ASN90 | |
J | ASN90 | |
B | GLN234 | |
B | ILE709 | |
C | GLN234 | |
C | ILE709 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
I | ASN103 | |
I | ASN432 | |
J | ASN103 | |
J | 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 |
I | ASN546 | |
J | ASN546 | |
C | PRO325 |
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 | VAL603 | |
B | VAL603 | |
C | VAL603 |
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 | HIS676 | |
A | SER678 | |
B | HIS676 | |
B | SER678 | |
C | HIS676 | |
C | SER678 |
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 | ASP1134 | |
B | ASP1134 | |
C | ASP1134 |