Research workbench
AlphaFold monomer V2.0 prediction for nucleolar protein 58 (P0CP26)
Analyse AlphaFold monomer V2.0 prediction for nucleolar protein 58 (P0CP26) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CP26
- Type
- protein
- Length
- 568 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe1a3255Eb5D00A44d1ac83ABb776899a5fE974ac
- Molecule
- Nucleolar protein 58
- UniProt
- P0CP26
- Pockets
- 5 · best druggability 0.41
Structure
1 distinct chain · 58% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleolar protein 58 | protein | 568 | 58% helix, 4% strand | P0CP26 |
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 | 154 | 0.41 | 0.74 | 21 | empty |
| 2 | 88 | 0.41 | 0.78 | 21 | empty |
| 3 | 60 | 0.37 | 0.79 | 16 | empty |
| 4 | 73 | 0.31 | 0.74 | 13 | empty |
| 5 | 52 | 0.25 | 0.73 | 10 | 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 P0CP26
- Elsewhere: UniProt P0CP26 · AlphaFold DB P0CP26
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