Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent rRNA helicase RRP3 (Q2UNB7)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent rRNA helicase RRP3 (Q2UNB7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2UNB7
- Type
- protein
- Length
- 472 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x99b776DEB2a7E235736ca77F71997f7A305AC803
- Molecule
- ATP-dependent rRNA helicase RRP3
- UniProt
- Q2UNB7
- Pockets
- 3 · best druggability 0.68
Structure
1 distinct chain · 43% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent rRNA helicase RRP3 | protein | 472 | 43% helix, 14% strand | Q2UNB7 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.68 | 0.83 | 39 | empty |
| 2 | 269 | 0.59 | 0.79 | 37 | empty |
| 3 | 298 | 0.58 | 0.77 | 39 | 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 Q2UNB7
- Elsewhere: UniProt Q2UNB7 · AlphaFold DB Q2UNB7
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