Research workbench
AlphaFold monomer V2.0 prediction for probable dual-specificity RNA methyltransferase rlmn (A7GG92)
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
- A7GG92
- Type
- protein
- Length
- 342 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- Probable dual-specificity RNA methyltransferase rlmn
- UniProt
- A7GG92
- Pockets
- 3 · best druggability 0.80
Structure
1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable dual-specificity RNA methyltransferase rlmn | protein | 342 | 39% helix, 22% strand | A7GG92 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.80 | 0.97 | 29 | empty |
| 2 | 52 | 0.60 | 0.92 | 18 | empty |
| 3 | 253 | 0.54 | 0.77 | 24 | 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 A7GG92
- Elsewhere: UniProt A7GG92 · AlphaFold DB A7GG92
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