Research workbench
AlphaFold monomer V2.0 prediction for nucleolar complex protein 4 homolog B (Q6NU91)
Analyse AlphaFold monomer V2.0 prediction for nucleolar complex protein 4 homolog B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6NU91
- Type
- protein
- Length
- 525 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc1787D436e4D305ADFB98fC66B68c7ee25625029
- Molecule
- Nucleolar complex protein 4 homolog B
- UniProt
- Q6NU91
- Pockets
- 4 · best druggability 0.49
Structure
1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleolar complex protein 4 homolog B | protein | 525 | 63% helix, 0% strand | Q6NU91 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.49 | 0.78 | 18 | empty |
| 2 | 95 | 0.40 | 0.77 | 23 | empty |
| 3 | 89 | 0.39 | 0.77 | 21 | empty |
| 4 | 80 | 0.30 | 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 Q6NU91
- Elsewhere: UniProt Q6NU91 · AlphaFold DB Q6NU91
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