Research workbench
AlphaFold monomer V2.0 prediction for dual-specificity RNA methyltransferase rlmn (B4TD95)
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
- B4TD95
- Type
- protein
- Length
- 388 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x537a7697cdcd278751bf40d02a88e497634048D7
- Molecule
- Dual-specificity RNA methyltransferase rlmn
- UniProt
- B4TD95
- Pockets
- 5 · best druggability 0.83
Structure
1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual-specificity RNA methyltransferase rlmn | protein | 388 | 38% helix, 18% strand | B4TD95 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 193 | 0.83 | 0.97 | 32 | empty |
| 2 | 393 | 0.67 | 0.80 | 42 | empty |
| 3 | 368 | 0.57 | 0.75 | 43 | empty |
| 4 | 53 | 0.44 | 0.84 | 16 | empty |
| 5 | 60 | 0.32 | 0.76 | 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 B4TD95
- Elsewhere: UniProt B4TD95 · AlphaFold DB B4TD95
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