Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase DBP2 (Q4X195)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase DBP2 (Q4X195) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4X195
- Type
- protein
- Length
- 547 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- ATP-dependent RNA helicase DBP2
- UniProt
- Q4X195
- Pockets
- 2 · best druggability 0.76
Structure
1 distinct chain · 34% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase DBP2 | protein | 547 | 34% helix, 12% strand | Q4X195 |
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 | 772 | 0.76 | 0.81 | 79 | empty |
| 2 | 157 | 0.44 | 0.75 | 21 | 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 Q4X195
- Elsewhere: UniProt Q4X195 · AlphaFold DB Q4X195
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