7TEX
Cryo-EM structure of SARS-CoV-2 Delta (B.1.617.2) spike protein in complex with human 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 |
| E | 0006508 | biological_process | proteolysis |
| E | 0008237 | molecular_function | metallopeptidase activity |
| E | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| E | 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 |
| E | 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 |
| E | GLU375 | |
| B | VAL687 | |
| C | VAL687 |
| 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 |
| E | HIS505 | |
| B | PRO817 | |
| C | PRO817 |
| 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 |
| E | ARG169 | |
| E | TRP477 | |
| E | LYS481 | |
| B | ASN17 | |
| B | THR1160 | |
| B | SER1175 | |
| C | ASN17 | |
| C | THR1160 | |
| C | SER1175 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| E | ARG273 | |
| B | THR1076 | |
| C | ASN61 | |
| C | ASN122 | |
| C | THR719 | |
| C | SER803 | |
| C | THR1076 | |
| E | HIS345 | |
| E | TYR515 | |
| A | SER803 | |
| A | THR1076 | |
| B | ASN61 | |
| B | ASN122 | |
| B | THR719 | |
| B | SER803 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
| Chain | Residue | Details |
| E | HIS374 | |
| E | HIS378 | |
| E | GLU402 | |
| B | ASN74 | |
| B | ASN151 | |
| B | SER1196 | |
| C | ASN74 | |
| C | ASN151 | |
| C | SER1196 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| E | ASN53 | |
| B | THR333 | |
| B | THR345 | |
| B | THR618 | |
| B | SER659 | |
| B | THR1100 | |
| C | THR167 | |
| C | THR284 | |
| C | THR333 | |
| C | THR345 | |
| C | THR618 | |
| E | ASN322 | |
| C | SER659 | |
| C | THR1100 | |
| A | THR333 | |
| A | THR345 | |
| A | THR618 | |
| A | SER659 | |
| A | THR1100 | |
| B | THR167 | |
| B | THR284 |
| 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 |
| E | ASN90 | |
| A | SER711 | |
| B | THR236 | |
| B | SER711 | |
| C | THR236 | |
| C | SER711 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
| Chain | Residue | Details |
| E | ASN103 | |
| E | ASN432 | |
| C | SER325 |
| 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 |
| E | ASN546 | |
| B | VAL327 | |
| C | VAL327 |
| 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 | SER605 | |
| B | SER605 | |
| C | SER605 |
| 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 | THR678 | |
| A | SER680 | |
| B | THR678 | |
| B | SER680 | |
| C | THR678 | |
| C | SER680 |
| 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 | THR1136 | |
| B | THR1136 | |
| C | THR1136 |
