Research workbench
AlphaFold monomer V2.0 prediction for nucleolar complex protein 3 homolog (Q91Y26)
Analyse AlphaFold monomer V2.0 prediction for nucleolar complex protein 3 homolog… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q91Y26
- Type
- protein
- Length
- 800 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4351fbBA2D1ce306FC22A21df5a9787370D5053a
- Molecule
- Nucleolar complex protein 3 homolog
- UniProt
- Q91Y26
- Pockets
- 7 · best druggability 0.59
Structure
1 distinct chain · 59% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleolar complex protein 3 homolog | protein | 800 | 59% helix, 2% strand | Q91Y26 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 252 | 0.59 | 0.79 | 26 | empty |
| 2 | 162 | 0.49 | 0.77 | 24 | empty |
| 3 | 72 | 0.45 | 0.82 | 16 | empty |
| 4 | 181 | 0.45 | 0.74 | 42 | empty |
| 5 | 64 | 0.38 | 0.78 | 17 | 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 Q91Y26
- Elsewhere: UniProt Q91Y26 · AlphaFold DB Q91Y26
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