Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent rRNA helicase RRP3 (P0CR00)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent rRNA helicase RRP3 (P0CR00) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CR00
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
- Molecule
- ATP-dependent rRNA helicase RRP3
- UniProt
- P0CR00
- Pockets
- 3 · best druggability 0.71
Structure
1 distinct chain · 40% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent rRNA helicase RRP3 | protein | 484 | 40% helix, 13% strand | P0CR00 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 765 | 0.71 | 0.78 | 63 | empty |
| 2 | 78 | 0.47 | 0.83 | 20 | empty |
| 3 | 60 | 0.30 | 0.75 | 15 | 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 P0CR00
- Elsewhere: UniProt P0CR00 · AlphaFold DB P0CR00
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