Research workbench
AlphaFold monomer V2.0 prediction for nucleolar protein 10 (Q66H99)
Analyse AlphaFold monomer V2.0 prediction for nucleolar protein 10 (Q66H99) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q66H99
- Type
- protein
- Length
- 688 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdE0734Aa6a66F7c5d25eE07fcCDE0b35ea4ccc4b
- Molecule
- Nucleolar protein 10
- UniProt
- Q66H99
- Pockets
- 7 · best druggability 0.74
Structure
1 distinct chain · 27% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleolar protein 10 | protein | 688 | 27% helix, 29% strand | Q66H99 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 817 | 0.74 | 0.79 | 62 | empty |
| 2 | 209 | 0.59 | 0.80 | 34 | empty |
| 3 | 108 | 0.50 | 0.81 | 23 | empty |
| 4 | 135 | 0.44 | 0.76 | 19 | empty |
| 5 | 125 | 0.41 | 0.75 | 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 Q66H99
- Elsewhere: UniProt Q66H99 · AlphaFold DB Q66H99
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