Research workbench
AlphaFold monomer V2.0 prediction for dual-specificity RNA methyltransferase rlmn (A5CX33)
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
- A5CX33
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x87aD4E3aa8116A59bb2fD5A498235D57C8a4cAaA
- Molecule
- Dual-specificity RNA methyltransferase rlmn
- UniProt
- A5CX33
- Pockets
- 3 · best druggability 0.83
Structure
1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual-specificity RNA methyltransferase rlmn | protein | 356 | 39% helix, 21% strand | A5CX33 |
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 | 204 | 0.83 | 0.97 | 32 | empty |
| 2 | 443 | 0.68 | 0.80 | 39 | empty |
| 3 | 51 | 0.29 | 0.75 | 14 | 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 A5CX33
- Elsewhere: UniProt A5CX33 · AlphaFold DB A5CX33
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