Research workbench
AlphaFold monomer V2.0 prediction for nucleolar protein 10 (Q5RJG1)
Analyse AlphaFold monomer V2.0 prediction for nucleolar protein 10 (Q5RJG1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5RJG1
- Type
- protein
- Length
- 687 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x12c6ba7fE4475e1AC24b8844Ed08A79eCC7B1e28
- Molecule
- Nucleolar protein 10
- UniProt
- Q5RJG1
- Pockets
- 5 · best druggability 0.74
Structure
1 distinct chain · 29% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleolar protein 10 | protein | 687 | 29% helix, 29% strand | Q5RJG1 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 849 | 0.74 | 0.78 | 60 | empty |
| 2 | 194 | 0.60 | 0.82 | 31 | empty |
| 3 | 106 | 0.51 | 0.82 | 21 | empty |
| 4 | 153 | 0.44 | 0.75 | 22 | empty |
| 5 | 96 | 0.36 | 0.74 | 19 | 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 Q5RJG1
- Elsewhere: UniProt Q5RJG1 · AlphaFold DB Q5RJG1
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