Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (Q31UK5)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase rhlb (Q31UK5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q31UK5
- Type
- protein
- Length
- 421 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- ATP-dependent RNA helicase rhlb
- UniProt
- Q31UK5
- Pockets
- 4 · best druggability 0.77
Structure
1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase rhlb | protein | 421 | 41% helix, 15% strand | Q31UK5 |
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 | 705 | 0.77 | 0.82 | 64 | empty |
| 2 | 118 | 0.38 | 0.74 | 21 | empty |
| 3 | 86 | 0.36 | 0.75 | 13 | empty |
| 4 | 74 | 0.29 | 0.72 | 17 | 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 Q31UK5
- Elsewhere: UniProt Q31UK5 · AlphaFold DB Q31UK5
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