7DQA
Cryo-EM structure of SARS-CoV2 RBD-ACE2 complex
Functional Information from GO Data
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 |
| A | THR371-GLN380 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942 |
| Chain | Residue | Details |
| C | ASN343 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU01354 |
| Chain | Residue | Details |
| A | ILE741-ILE761 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 43 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| A | PHE762-PHE805 |
| site_id | SWS_FT_FI4 |
| 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 |
| A | GLU375 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| A | HIS505 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774 |
| Chain | Residue | Details |
| A | ARG169 | |
| A | TRP477 | |
| A | LYS481 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| A | ARG273 | |
| A | HIS345 | |
| A | TYR515 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895 |
| Chain | Residue | Details |
| A | HIS374 | |
| A | HIS378 | |
| A | GLU402 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498 |
| Chain | Residue | Details |
| A | TYR781 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498 |
| Chain | Residue | Details |
| A | SER783 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895 |
| Chain | Residue | Details |
| A | ASN53 | |
| A | ASN322 |
| site_id | SWS_FT_FI12 |
| 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 |
| A | ASN90 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895 |
| Chain | Residue | Details |
| A | ASN103 | |
| A | ASN432 |
| site_id | SWS_FT_FI14 |
| 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 |
| A | ASN546 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN690 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36876523 |
| Chain | Residue | Details |
| A | LYS788 |
