Research workbench
AlphaFold monomer V2.0 prediction for nucleolar protein 58 (A6ZPE5)
Analyse AlphaFold monomer V2.0 prediction for nucleolar protein 58 (A6ZPE5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A6ZPE5
- Type
- protein
- Length
- 511 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3003814e7Ab117c7f42c4cd35Ec37B49DB1a1C15
- Molecule
- Nucleolar protein 58
- UniProt
- A6ZPE5
- Pockets
- 2 · best druggability 0.34
Structure
1 distinct chain · 59% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleolar protein 58 | protein | 511 | 59% helix, 5% strand | A6ZPE5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.34 | 0.74 | 19 | empty |
| 2 | 65 | 0.31 | 0.74 | 16 | empty |
Compared structures
- 7SUK · Structure of Bfr2-Lcp5 Complex Observed in the Small Subunit Processome Isolated from… · an experimental structure of the same protein · chain A against SB, TM-score 0.80
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 A6ZPE5
- Elsewhere: UniProt A6ZPE5 · AlphaFold DB A6ZPE5
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