Research workbench
AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase RIO1 (O42650)
Analyse AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase RIO1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O42650
- Type
- protein
- Length
- 497 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x822BfDB52f100Af7414C872a89eE1bfF1069766B
- Molecule
- SERINE/THREONINE-protein kinase RIO1
- UniProt
- O42650
- Pockets
- 6 · best druggability 0.69
Structure
1 distinct chain · 37% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase RIO1 | protein | 497 | 37% helix, 10% strand | O42650 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 296 | 0.69 | 0.83 | 35 | empty |
| 2 | 560 | 0.64 | 0.75 | 50 | empty |
| 3 | 81 | 0.43 | 0.80 | 16 | empty |
| 4 | 79 | 0.36 | 0.76 | 15 | empty |
| 5 | 74 | 0.34 | 0.76 | 16 | 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 O42650
- Elsewhere: UniProt O42650 · AlphaFold DB O42650
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