Research workbench
AlphaFold monomer V2.0 prediction for ring finger protein 121 (Q9H920)
Analyse AlphaFold monomer V2.0 prediction for ring finger protein 121 (Q9H920) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9H920
- Type
- protein
- Length
- 327 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC059994D9AcD9d2974016E55c136a479A61DC795
- Molecule
- Ring finger protein 121
- UniProt
- Q9H920
- Pockets
- 6 · best druggability 0.62
Structure
1 distinct chain · 67% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ring finger protein 121 | protein | 327 | 67% helix, 3% strand | Q9H920 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 246 | 0.62 | 0.81 | 35 | empty |
| 2 | 102 | 0.40 | 0.76 | 18 | empty |
| 3 | 54 | 0.36 | 0.78 | 12 | empty |
| 4 | 66 | 0.33 | 0.76 | 15 | empty |
| 5 | 60 | 0.31 | 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 Q9H920
- Elsewhere: UniProt Q9H920 · AlphaFold DB Q9H920
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