Research workbench
AlphaFold monomer V2.0 prediction for probable dual-specificity RNA methyltransferase rlmn (B5YF42)
Analyse AlphaFold monomer V2.0 prediction for probable dual-specificity RNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5YF42
- Type
- protein
- Length
- 348 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- Probable dual-specificity RNA methyltransferase rlmn
- UniProt
- B5YF42
- Pockets
- 3 · best druggability 0.83
Structure
1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable dual-specificity RNA methyltransferase rlmn | protein | 348 | 39% helix, 21% strand | B5YF42 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 200 | 0.83 | 0.96 | 31 | empty |
| 2 | 284 | 0.62 | 0.80 | 33 | empty |
| 3 | 50 | 0.35 | 0.79 | 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 B5YF42
- Elsewhere: UniProt B5YF42 · AlphaFold DB B5YF42
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