Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RING1 (A1YFY1)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RING1 (A1YFY1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1YFY1
- Type
- protein
- Length
- 377 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- E3 ubiquitin-protein ligase RING1
- UniProt
- A1YFY1
- Pockets
- 2 · best druggability 0.32
Structure
1 distinct chain · 29% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase RING1 | protein | 377 | 29% helix, 12% strand | A1YFY1 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.32 | 0.74 | 16 | empty |
| 2 | 58 | 0.29 | 0.74 | 11 | 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 A1YFY1
- Elsewhere: UniProt A1YFY1 · AlphaFold DB A1YFY1
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