Research workbench
AlphaFold monomer V2.0 prediction for nucleolar complex protein 4 homolog (Q4VBT2)
Analyse AlphaFold monomer V2.0 prediction for nucleolar complex protein 4 homolog… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4VBT2
- Type
- protein
- Length
- 525 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Nucleolar complex protein 4 homolog
- UniProt
- Q4VBT2
- Pockets
- 5 · best druggability 0.44
Structure
1 distinct chain · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleolar complex protein 4 homolog | protein | 525 | 65% helix, 0% strand | Q4VBT2 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.44 | 0.78 | 23 | empty |
| 2 | 93 | 0.37 | 0.75 | 22 | empty |
| 3 | 61 | 0.31 | 0.75 | 18 | empty |
| 4 | 83 | 0.30 | 0.73 | 16 | empty |
| 5 | 74 | 0.29 | 0.72 | 18 | 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 Q4VBT2
- Elsewhere: UniProt Q4VBT2 · AlphaFold DB Q4VBT2
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