Research workbench
AlphaFold monomer V2.0 prediction for 23S rRNA (URACIL(1939)-C(5))-methyltransferase rlmd (Q5E320)
Analyse AlphaFold monomer V2.0 prediction for 23S rRNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5E320
- Type
- protein
- Length
- 438 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xddD89F6cedc3679f21663f3046B4aB3D5161E34E
- Molecule
- 23S rRNA (URACIL(1939)-C(5))-methyltransferase rlmd
- UniProt
- Q5E320
- Pockets
- 2 · best druggability 0.71
Structure
1 distinct chain · 24% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 23S rRNA (URACIL(1939)-C(5))-methyltransferase rlmd | protein | 438 | 24% helix, 32% strand | Q5E320 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 721 | 0.71 | 0.78 | 84 | empty |
| 2 | 145 | 0.51 | 0.79 | 31 | 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 Q5E320
- Elsewhere: UniProt Q5E320 · AlphaFold DB Q5E320
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