Research workbench
AlphaFold monomer V2.0 prediction for ring finger protein 10 (Q5XI59)
Analyse AlphaFold monomer V2.0 prediction for ring finger protein 10 (Q5XI59) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5XI59
- Type
- protein
- Length
- 802 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA40142fE4BDa34A12E7e506aD8115eEBb8b9eedb
- Molecule
- Ring finger protein 10
- UniProt
- Q5XI59
- Pockets
- 5 · best druggability 0.75
Structure
1 distinct chain · 21% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ring finger protein 10 | protein | 802 | 21% helix, 10% strand | Q5XI59 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 698 | 0.75 | 0.81 | 72 | empty |
| 2 | 375 | 0.58 | 0.75 | 43 | empty |
| 3 | 160 | 0.47 | 0.76 | 20 | empty |
| 4 | 89 | 0.40 | 0.77 | 19 | empty |
| 5 | 55 | 0.25 | 0.72 | 14 | 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 Q5XI59
- Elsewhere: UniProt Q5XI59 · AlphaFold DB Q5XI59
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