Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent rRNA helicase RRP3 (P38712)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent rRNA helicase RRP3 (P38712) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P38712
- Type
- protein
- Length
- 501 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xba5fB0D21f0B04Cdf2D70FE38daDdF696FDB8152
- Molecule
- ATP-dependent rRNA helicase RRP3
- UniProt
- P38712
- Pockets
- 7 · best druggability 0.61
Structure
1 distinct chain · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent rRNA helicase RRP3 | protein | 501 | 49% helix, 13% strand | P38712 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 207 | 0.61 | 0.82 | 35 | empty |
| 2 | 244 | 0.58 | 0.79 | 28 | empty |
| 3 | 79 | 0.46 | 0.81 | 14 | empty |
| 4 | 88 | 0.45 | 0.80 | 17 | empty |
| 5 | 151 | 0.41 | 0.74 | 18 | 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 P38712
- Elsewhere: UniProt P38712 · AlphaFold DB P38712
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.