Research workbench
Crystal structure of phosphorylated ret tyrosine kinase domain complexed with the inhibitor PP1
Analyse Crystal structure of phosphorylated ret tyrosine kinase domain complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IVV
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proto-oncogene tyrosine-protein kinase receptor ret precursor
- EC
- 2.7.10.1
- UniProt
- P07949
- Ligands
- PP1
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proto-oncogene tyrosine-protein kinase receptor ret precursor (EC 2.7.10.1) | protein | 283 | 42% helix, 19% strand | P07949 |
Ligands and binding sites
- PP1 · 1-ter-butyl-3-P-tolyl-1H-pyrazolo[3,4-d]pyrimidin-4-ylamine · ligand · chains A
- FMT · Formic acid · additive · 2 copies · 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 | 313 | 0.69 | 0.83 | 38 | PP1 |
| 2 | 53 | 0.26 | 0.73 | 11 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 2IVV · Crystal structure of phosphorylated RET tyrosine kinase domain complexed with the… · 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 0.94
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 2IVV · PDBe 2IVV · UniProt P07949
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