Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent rRNA helicase RRP3 (A7EML8)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent rRNA helicase RRP3 (A7EML8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7EML8
- Type
- protein
- Length
- 482 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6c05b483540F55289d602403d0273aF68B0db5F9
- Molecule
- ATP-dependent rRNA helicase RRP3
- UniProt
- A7EML8
- Pockets
- 4 · best druggability 0.66
Structure
1 distinct chain · 41% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent rRNA helicase RRP3 | protein | 482 | 41% helix, 14% strand | A7EML8 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 249 | 0.66 | 0.83 | 39 | empty |
| 2 | 62 | 0.60 | 0.91 | 19 | empty |
| 3 | 210 | 0.56 | 0.80 | 31 | empty |
| 4 | 325 | 0.53 | 0.74 | 26 | 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 A7EML8
- Elsewhere: UniProt A7EML8 · AlphaFold DB A7EML8
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