Research workbench
AlphaFold monomer V2.0 prediction for dual-specificity RNA methyltransferase rlmn (A4IY03)
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
- A4IY03
- Type
- protein
- Length
- 370 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35cE46a4a30196447966Bd34E1e090Eb6D1bAd3f
- Molecule
- Dual-specificity RNA methyltransferase rlmn
- UniProt
- A4IY03
- Pockets
- 3 · best druggability 0.82
Structure
1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual-specificity RNA methyltransferase rlmn | protein | 370 | 41% helix, 19% strand | A4IY03 |
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 | 190 | 0.82 | 0.96 | 32 | empty |
| 2 | 365 | 0.70 | 0.82 | 36 | empty |
| 3 | 82 | 0.33 | 0.74 | 15 | 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 A4IY03
- Elsewhere: UniProt A4IY03 · AlphaFold DB A4IY03
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