Research workbench
AlphaFold monomer V2.0 prediction for dual-specificity RNA methyltransferase rlmn (B1IWE4)
Analyse AlphaFold monomer V2.0 prediction for dual-specificity RNA methyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1IWE4
- Type
- protein
- Length
- 384 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- Dual-specificity RNA methyltransferase rlmn
- UniProt
- B1IWE4
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual-specificity RNA methyltransferase rlmn | protein | 384 | 39% helix, 18% strand | B1IWE4 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 568 | 0.80 | 0.86 | 62 | empty |
| 2 | 304 | 0.54 | 0.75 | 37 | empty |
| 3 | 196 | 0.47 | 0.75 | 25 | empty |
| 4 | 93 | 0.38 | 0.77 | 19 | 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 B1IWE4
- Elsewhere: UniProt B1IWE4 · AlphaFold DB B1IWE4
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