7XBF
The complex structure of RshSTT182/200 RBD-insert2 bound to human ACE2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| A | 0016020 | cellular_component | membrane |
| C | 0006508 | biological_process | proteolysis |
| C | 0008237 | molecular_function | metallopeptidase activity |
| C | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| C | 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 |
| A | THR371-GLN380 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1176 |
| Details | Domain: {"description":"Peptidase M2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | Region: {"description":"Interaction with SARS-CoV spike glycoprotein","evidences":[{"source":"PubMed","id":"15791205","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27217402","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19021774","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19901337","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14754895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19901337","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
