7R1A
Furin Cleaved Alpha Variant SARS-CoV-2 Spike in complex with 3 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 |
D | 0006508 | biological_process | proteolysis |
D | 0008237 | molecular_function | metallopeptidase activity |
D | 0008241 | molecular_function | peptidyl-dipeptidase activity |
D | 0016020 | cellular_component | membrane |
E | 0006508 | biological_process | proteolysis |
E | 0008237 | molecular_function | metallopeptidase activity |
E | 0008241 | molecular_function | peptidyl-dipeptidase activity |
E | 0016020 | cellular_component | membrane |
F | 0006508 | biological_process | proteolysis |
F | 0008237 | molecular_function | metallopeptidase activity |
F | 0008241 | molecular_function | peptidyl-dipeptidase activity |
F | 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 | 3 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402 |
Chain | Residue | Details |
D | GLU375 | |
E | GLU375 | |
F | GLU375 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
D | HIS505 | |
E | HIS505 | |
F | HIS505 |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
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 | |
E | ARG169 | |
E | TRP477 | |
E | LYS481 | |
F | ARG169 | |
F | TRP477 | |
F | LYS481 |
site_id | SWS_FT_FI4 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
D | ARG273 | |
B | THR1077 | |
C | ASN61 | |
C | THR124 | |
C | ILE720 | |
C | GLN804 | |
C | THR1077 | |
D | HIS345 | |
D | TYR515 | |
E | ARG273 | |
E | HIS345 | |
E | TYR515 | |
F | ARG273 | |
F | HIS345 | |
F | TYR515 |
site_id | SWS_FT_FI5 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
D | HIS374 | |
D | HIS378 | |
D | GLU402 | |
E | HIS374 | |
E | HIS378 | |
E | GLU402 | |
F | HIS374 | |
F | HIS378 | |
F | GLU402 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
D | ASN53 | |
B | ASN334 | |
B | ARG346 | |
B | GLU619 | |
B | TYR660 | |
B | HIS1101 | |
C | PHE168 | |
C | ILE285 | |
C | ASN334 | |
C | ARG346 | |
C | GLU619 | |
D | ASN322 | |
C | TYR660 | |
C | HIS1101 | |
E | ASN53 | |
E | ASN322 | |
F | ASN53 | |
F | ASN322 | |
A | HIS1101 | |
B | PHE168 | |
B | ILE285 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337 |
Chain | Residue | Details |
D | ASN90 | |
E | ASN90 | |
F | ASN90 | |
B | ILE712 | |
C | ARG237 | |
C | ILE712 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
D | ASN103 | |
D | ASN432 | |
E | ASN103 | |
E | ASN432 | |
F | ASN103 | |
F | ASN432 |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337 |
Chain | Residue | Details |
D | ASN546 | |
E | ASN546 | |
F | ASN546 |
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 | ASN606 | |
B | ASN606 | |
C | ASN606 |
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 | ASN679 | |
A | HIS681 | |
B | ASN679 | |
B | HIS681 | |
C | ASN679 | |
C | HIS681 |
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 | VAL1137 | |
B | VAL1137 | |
C | VAL1137 |