Research workbench
AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase tousled (Q39238)
Analyse AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase tousled… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q39238
- Type
- protein
- Length
- 688 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- SERINE/THREONINE-protein kinase tousled
- UniProt
- Q39238
- Pockets
- 4 · best druggability 0.82
Structure
1 distinct chain · 40% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase tousled | protein | 688 | 40% helix, 11% strand | Q39238 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 925 | 0.82 | 0.84 | 95 | empty |
| 2 | 219 | 0.51 | 0.76 | 25 | empty |
| 3 | 71 | 0.38 | 0.78 | 19 | empty |
| 4 | 54 | 0.33 | 0.78 | 17 | empty |
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 Q39238
- Elsewhere: UniProt Q39238 · AlphaFold DB Q39238
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