Research workbench
AlphaFold monomer V2.0 prediction for 50S ribosomal protein L25 (Q92F64)
Analyse AlphaFold monomer V2.0 prediction for 50S ribosomal protein L25 (Q92F64) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q92F64
- Type
- protein
- Length
- 207 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- 50S ribosomal protein L25
- UniProt
- Q92F64
- Pockets
- 1 · best druggability 0.30
Structure
1 distinct chain · 13% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 50S ribosomal protein L25 | protein | 207 | 13% helix, 42% strand | Q92F64 |
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 | 53 | 0.30 | 0.75 | 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 Q92F64
- Elsewhere: UniProt Q92F64 · AlphaFold DB Q92F64
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