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 adhesion via plasma membrane adhesion molecules |
| E | 0016020 | cellular_component | membrane |
| F | 0005509 | molecular_function | calcium ion binding |
| F | 0007156 | biological_process | homophilic cell adhesion via plasma membrane adhesion molecules |
| F | 0016020 | cellular_component | membrane |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1212 |
| Details | TOPO_DOM: Extracellular => ECO:0000255 |
| Chain | Residue | Details |
| E | LEU29-ARG635 | |
| F | LEU29-ARG635 | |
| D | ASN52 | |
| D | ASN357 | |
| B | ARG149 | |
| B | ARG158 | |
| B | ARG160 | |
| B | GLN162 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31535977, ECO:0000305|PubMed:25242331, ECO:0007744|PDB:4UX8, ECO:0007744|PDB:6Q2J |
| Chain | Residue | Details |
| E | GLU178 | |
| F | ASP230 | |
| F | ASP264 | |
| F | GLU265 | |
| F | ASP266 | |
| F | SER268 | |
| F | ASP300 | |
| F | ASP302 | |
| E | ASP230 | |
| E | ASP264 | |
| E | GLU265 | |
| E | ASP266 | |
| E | SER268 | |
| E | ASP300 | |
| E | ASP302 | |
| F | GLU178 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31535977, ECO:0007744|PDB:6Q2J |
| Chain | Residue | Details |
| E | ASN179 | |
| E | ASP584 | |
| F | ASN179 | |
| F | GLU232 | |
| F | ASP267 | |
| F | ASP378 | |
| F | THR564 | |
| F | CYS565 | |
| F | ASP567 | |
| F | HIS569 | |
| F | GLU574 | |
| E | GLU232 | |
| F | ASP584 | |
| E | ASP267 | |
| E | ASP378 | |
| E | THR564 | |
| E | CYS565 | |
| E | ASP567 | |
| E | HIS569 | |
| E | GLU574 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Breakpoint for translocation to form the TRIM27/RET oncogene => ECO:0000269|PubMed:3037315 |
| Chain | Residue | Details |
| E | ARG587 | |
| F | ARG587 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 22 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| E | ASN98 | |
| E | ASN468 | |
| E | ASN554 | |
| F | ASN98 | |
| F | ASN199 | |
| F | ASN336 | |
| F | ASN343 | |
| F | ASN361 | |
| F | ASN367 | |
| F | ASN377 | |
| F | ASN394 | |
| E | ASN199 | |
| F | ASN448 | |
| F | ASN468 | |
| F | ASN554 | |
| E | ASN336 | |
| E | ASN343 | |
| E | ASN361 | |
| E | ASN367 | |
| E | ASN377 | |
| E | ASN394 | |
| E | ASN448 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20473317 |
| Chain | Residue | Details |
| E | ASN151 | |
| F | ASN151 |
