Research workbench
AlphaFold monomer V2.0 prediction for nucleolar protein 11-like (Q4V9P9)
Analyse AlphaFold monomer V2.0 prediction for nucleolar protein 11-like (Q4V9P9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4V9P9
- Type
- protein
- Length
- 708 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- Molecule
- Nucleolar protein 11-like
- UniProt
- Q4V9P9
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleolar protein 11-like | protein | 708 | 30% helix, 27% strand | Q4V9P9 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 723 | 0.70 | 0.77 | 68 | empty |
| 2 | 421 | 0.64 | 0.78 | 54 | empty |
| 3 | 133 | 0.50 | 0.79 | 21 | empty |
| 4 | 59 | 0.26 | 0.72 | 13 | 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 Q4V9P9
- Elsewhere: UniProt Q4V9P9 · AlphaFold DB Q4V9P9
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