Research workbench
AlphaFold monomer V2.0 prediction for ribosomal protein L11 methyltransferase (A5F3S3)
Analyse AlphaFold monomer V2.0 prediction for ribosomal protein L11 methyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5F3S3
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- Ribosomal protein L11 methyltransferase
- UniProt
- A5F3S3
- Pockets
- 2 · best druggability 0.71
Structure
1 distinct chain · 31% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosomal protein L11 methyltransferase | protein | 295 | 31% helix, 29% strand | A5F3S3 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 904 | 0.71 | 0.75 | 68 | empty |
| 2 | 160 | 0.54 | 0.80 | 20 | 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 A5F3S3
- Elsewhere: UniProt A5F3S3 · AlphaFold DB A5F3S3
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