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Crystal structure of hyper-phosphorylated RET kinase domain with (proximal) juxtamembrane segment
Analyse Crystal structure of hyper-phosphorylated RET kinase domain with (proximal)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FM2
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.3
- Source
- HOMO SAPIENS
- Molecule
- Proto-oncogene tyrosine-protein kinase receptor ret
- EC
- 2.7.10.1
- UniProt
- P07949
- Ligands
- PP1
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · resolution 3.3 · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proto-oncogene tyrosine-protein kinase receptor ret (EC 2.7.10.1) | protein | 277 | 39% helix, 18% strand | P07949 |
Ligands and binding sites
- PP1 · 1-ter-butyl-3-P-tolyl-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 368 | 0.69 | 0.81 | 45 | PP1 |
| 2 | 150 | 0.39 | 0.73 | 19 | empty |
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 5FM2 · Crystal structure of hyper-phosphorylated ret kinase domain with (proximal) juxtamembrane… · the same entry in another collection · chain A against A, TM-score 1.00
- P07949 · AlphaFold monomer V2.0 prediction for proto-oncogene tyrosine-protein kinase receptor ret… · a predicted model of the same protein · chain A against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P07949
- Elsewhere: RCSB PDB 5FM2 · PDBe 5FM2 · UniProt P07949
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