Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (A5UDI1)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (A5UDI1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5UDI1
- Type
- protein
- Length
- 415 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- ATP-dependent RNA helicase rhlb
- UniProt
- A5UDI1
- Pockets
- 2 · best druggability 0.78
Structure
1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase rhlb | protein | 415 | 41% helix, 16% strand | A5UDI1 |
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 | 833 | 0.78 | 0.81 | 77 | empty |
| 2 | 117 | 0.40 | 0.76 | 23 | 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 A5UDI1
- Elsewhere: UniProt A5UDI1 · AlphaFold DB A5UDI1
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