6ACJ
Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 2
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 |
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 | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402 |
Chain | Residue | Details |
D | GLU375 | |
B | SER14-PRO1195 | |
C | SER14-PRO1195 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
D | HIS505 | |
A | ARG797 | |
B | ARG667 | |
B | ARG797 | |
C | ARG667 | |
C | ARG797 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774 |
Chain | Residue | Details |
D | ARG169 | |
A | ASN318 | |
A | ASN330 | |
A | ASN357 | |
A | ASN589 | |
A | ASN602 | |
A | ASN691 | |
A | ASN699 | |
A | ASN783 | |
A | ASN1056 | |
A | ASN1080 | |
D | TRP477 | |
A | ASN1116 | |
A | ASN1140 | |
A | ASN1155 | |
A | ASN1176 | |
B | ASN29 | |
B | ASN65 | |
B | ASN73 | |
B | ASN109 | |
B | ASN118 | |
B | ASN119 | |
D | LYS481 | |
B | ASN158 | |
B | ASN227 | |
B | ASN269 | |
B | ASN318 | |
B | ASN330 | |
B | ASN357 | |
B | ASN589 | |
B | ASN602 | |
B | ASN691 | |
B | ASN699 | |
A | ASN109 | |
B | ASN783 | |
B | ASN1056 | |
B | ASN1080 | |
B | ASN1116 | |
B | ASN1140 | |
B | ASN1155 | |
B | ASN1176 | |
C | ASN29 | |
C | ASN65 | |
C | ASN73 | |
A | ASN118 | |
C | ASN109 | |
C | ASN118 | |
C | ASN119 | |
C | ASN158 | |
C | ASN227 | |
C | ASN269 | |
C | ASN318 | |
C | ASN330 | |
C | ASN357 | |
C | ASN589 | |
A | ASN119 | |
C | ASN602 | |
C | ASN691 | |
C | ASN699 | |
C | ASN783 | |
C | ASN1056 | |
C | ASN1080 | |
C | ASN1116 | |
C | ASN1140 | |
C | ASN1155 | |
C | ASN1176 | |
A | ASN158 | |
A | ASN227 | |
A | ASN269 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
D | ARG273 | |
D | HIS345 | |
D | TYR515 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
Chain | Residue | Details |
D | HIS374 | |
D | HIS378 | |
D | GLU402 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
Chain | Residue | Details |
D | ASN53 | |
D | ASN322 |
site_id | SWS_FT_FI7 |
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 |
D | ASN90 |
site_id | SWS_FT_FI8 |
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_FI9 |
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 |