Research workbench
AlphaFold monomer V2.0 prediction for 40S ribosomal protein S26 (P61251)
Analyse AlphaFold monomer V2.0 prediction for 40S ribosomal protein S26 (P61251) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P61251
- Type
- protein
- Length
- 115 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- 40S ribosomal protein S26
- UniProt
- P61251
- Pockets
- 1 · best druggability 0.48
Structure
1 distinct chain · 12% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 40S ribosomal protein S26 | protein | 115 | 12% helix, 19% strand | P61251 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 231 | 0.48 | 0.74 | 25 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7SYH · Structure of the HCV ires binding to the 40S ribosomal subunit, closed conformation.… · an experimental structure of the same protein · chain A against b, TM-score 0.83
- 7SYH · Structure of the HCV IRES binding to the 40S ribosomal subunit, closed conformation.… · an experimental structure of the same protein · chain A against b, TM-score 0.83
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 P61251
- Elsewhere: UniProt P61251 · AlphaFold DB P61251
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