Research workbench
AlphaFold monomer V2.0 prediction for radiation-sensitive protein 28 (Q12021)
Analyse AlphaFold monomer V2.0 prediction for radiation-sensitive protein 28 (Q12021) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12021
- Type
- protein
- Length
- 506 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- Radiation-sensitive protein 28
- UniProt
- Q12021
- Pockets
- 5 · best druggability 0.72
Structure
1 distinct chain · 9% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Radiation-sensitive protein 28 | protein | 506 | 9% helix, 37% strand | Q12021 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 501 | 0.72 | 0.81 | 38 | empty |
| 2 | 108 | 0.46 | 0.79 | 26 | empty |
| 3 | 188 | 0.44 | 0.74 | 21 | empty |
| 4 | 98 | 0.34 | 0.73 | 19 | empty |
| 5 | 61 | 0.30 | 0.74 | 12 | 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 Q12021
- Elsewhere: UniProt Q12021 · AlphaFold DB Q12021
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