6Q2O
Cryo-EM structure of RET/GFRa2/NRTN extracellular complex. The 3D refinement was applied with C2 symmetry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008083 | molecular_function | growth factor activity |
| A | 0030116 | molecular_function | glial cell-derived neurotrophic factor receptor binding |
| A | 0030971 | molecular_function | receptor tyrosine kinase binding |
| B | 0008083 | molecular_function | growth factor activity |
| B | 0030116 | molecular_function | glial cell-derived neurotrophic factor receptor binding |
| B | 0030971 | molecular_function | receptor tyrosine kinase binding |
| C | 0038023 | molecular_function | signaling receptor activity |
| D | 0038023 | molecular_function | signaling receptor activity |
| E | 0005509 | molecular_function | calcium ion binding |
| E | 0007156 | biological_process | homophilic cell-cell adhesion |
| E | 0016020 | cellular_component | membrane |
| F | 0005509 | molecular_function | calcium ion binding |
| F | 0007156 | biological_process | homophilic cell-cell adhesion |
| F | 0016020 | cellular_component | membrane |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29414779","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 228 |
| Details | Region: {"description":"Cadherin-like region 3 (CLD3)","evidences":[{"source":"PubMed","id":"11445581","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 202 |
| Details | Region: {"description":"Cadherin-like region 4 (CLD4)","evidences":[{"source":"PubMed","id":"11445581","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31535977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25242331","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4UX8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q2J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31535977","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6Q2J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Breakpoint for translocation to form the TRIM27/RET oncogene","evidences":[{"source":"PubMed","id":"3037315","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20473317","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
