Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (Q1CBQ4)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (Q1CBQ4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1CBQ4
- Type
- protein
- Length
- 428 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x505a54e9c891975EBe9bE0abfDFa4150AA989521
- Molecule
- ATP-dependent RNA helicase rhlb
- UniProt
- Q1CBQ4
- Pockets
- 4 · best druggability 0.79
Structure
1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase rhlb | protein | 428 | 40% helix, 15% strand | Q1CBQ4 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 773 | 0.79 | 0.83 | 79 | empty |
| 2 | 106 | 0.45 | 0.78 | 16 | empty |
| 3 | 114 | 0.39 | 0.75 | 22 | empty |
| 4 | 70 | 0.30 | 0.73 | 15 | 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 Q1CBQ4
- Elsewhere: UniProt Q1CBQ4 · AlphaFold DB Q1CBQ4
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