Research workbench
AlphaFold monomer V2.0 prediction for ribosome assembly protein RRB1 (Q04225)
Analyse AlphaFold monomer V2.0 prediction for ribosome assembly protein RRB1 (Q04225) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q04225
- Type
- protein
- Length
- 511 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Ribosome assembly protein RRB1
- UniProt
- Q04225
- Pockets
- 6 · best druggability 0.77
Structure
1 distinct chain · 12% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosome assembly protein RRB1 | protein | 511 | 12% helix, 35% strand | Q04225 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 655 | 0.77 | 0.82 | 74 | empty |
| 2 | 231 | 0.53 | 0.76 | 34 | empty |
| 3 | 187 | 0.49 | 0.76 | 24 | empty |
| 4 | 100 | 0.34 | 0.73 | 17 | empty |
| 5 | 75 | 0.31 | 0.74 | 20 | 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 Q04225
- Elsewhere: UniProt Q04225 · AlphaFold DB Q04225
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