Research workbench
AlphaFold monomer V2.0 prediction for tyrosine-protein kinase yes (Q28923)
Analyse AlphaFold monomer V2.0 prediction for tyrosine-protein kinase yes (Q28923) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q28923
- Type
- protein
- Length
- 539 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x980069a966b7acEC19edb9933A7b9398958617B9
- Molecule
- Tyrosine-protein kinase yes
- UniProt
- Q28923
- Pockets
- 6 · best druggability 0.73
Structure
1 distinct chain · 26% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase yes | protein | 539 | 26% helix, 19% strand | Q28923 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.73 | 0.88 | 40 | empty |
| 2 | 608 | 0.72 | 0.80 | 63 | empty |
| 3 | 367 | 0.65 | 0.80 | 41 | empty |
| 4 | 209 | 0.55 | 0.79 | 40 | empty |
| 5 | 110 | 0.43 | 0.77 | 19 | 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 Q28923
- Elsewhere: UniProt Q28923 · AlphaFold DB Q28923
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