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Crystal structure of ret tyrosine kinase domain bound to adenosine
Analyse Crystal structure of ret tyrosine kinase domain bound to adenosine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CKJ
- Type
- protein
- Length
- 293 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proto-oncogene tyrosine-protein kinase receptor ret
- EC
- 2.7.10.1
- UniProt
- P07949
- Ligands
- ADN
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proto-oncogene tyrosine-protein kinase receptor ret (EC 2.7.10.1) | protein | 293 | 41% helix, 20% strand | P07949 |
Ligands and binding sites
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 | 386 | 0.67 | 0.80 | 35 | ADN, FMT |
| 2 | 125 | 0.42 | 0.76 | 26 | FMT |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 4CKJ · Crystal structure of RET tyrosine kinase domain bound to adenosine · 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 0.93
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 4CKJ · PDBe 4CKJ · UniProt P07949
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