Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent rRNA helicase RRP3 (A3LS22)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent rRNA helicase RRP3 (A3LS22) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3LS22
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- ATP-dependent rRNA helicase RRP3
- UniProt
- A3LS22
- Pockets
- 5 · best druggability 0.65
Structure
1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent rRNA helicase RRP3 | protein | 484 | 48% helix, 14% strand | A3LS22 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.65 | 0.93 | 24 | empty |
| 2 | 208 | 0.57 | 0.80 | 33 | empty |
| 3 | 118 | 0.41 | 0.76 | 23 | empty |
| 4 | 90 | 0.34 | 0.74 | 19 | empty |
| 5 | 51 | 0.33 | 0.78 | 12 | 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 A3LS22
- Elsewhere: UniProt A3LS22 · AlphaFold DB A3LS22
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