Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (A5F3R4)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (A5F3R4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5F3R4
- Type
- protein
- Length
- 438 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB5268aA94a7047738311f34fD805c7fe3F299d8D
- Molecule
- ATP-dependent RNA helicase rhlb
- UniProt
- A5F3R4
- Pockets
- 2 · best druggability 0.76
Structure
1 distinct chain · 38% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase rhlb | protein | 438 | 38% helix, 14% strand | A5F3R4 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 974 | 0.76 | 0.79 | 82 | empty |
| 2 | 73 | 0.29 | 0.73 | 16 | 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 A5F3R4
- Elsewhere: UniProt A5F3R4 · AlphaFold DB A5F3R4
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