Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (Q65RG7)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (Q65RG7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q65RG7
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8a4Ce783c76eba0951366Db8621c15D90cD3B4a6
- Molecule
- ATP-dependent RNA helicase rhlb
- UniProt
- Q65RG7
- Pockets
- 4 · best druggability 0.77
Structure
1 distinct chain · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase rhlb | protein | 417 | 40% helix, 16% strand | Q65RG7 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 793 | 0.77 | 0.81 | 68 | empty |
| 2 | 82 | 0.52 | 0.85 | 16 | empty |
| 3 | 113 | 0.41 | 0.76 | 21 | empty |
| 4 | 68 | 0.28 | 0.72 | 14 | 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 Q65RG7
- Elsewhere: UniProt Q65RG7 · AlphaFold DB Q65RG7
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