Research workbench
AlphaFold monomer V2.0 prediction for arginine-glutamic acid dipeptide repeats protein (Q80TZ9)
Analyse AlphaFold monomer V2.0 prediction for arginine-glutamic acid dipeptide repeats… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q80TZ9
- Type
- protein
- Length
- 1,558 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEa58c7534E5701aA8370E0fAEb19b7e14653e69c
- Molecule
- Arginine-glutamic acid dipeptide repeats protein
- UniProt
- Q80TZ9
- Pockets
- 11 · best druggability 0.60
Structure
1 distinct chain · 21% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine-glutamic acid dipeptide repeats protein | protein | 1558 | 21% helix, 6% strand | Q80TZ9 |
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 457 | 0.60 | 0.75 | 43 | empty |
| 2 | 202 | 0.51 | 0.77 | 23 | empty |
| 3 | 170 | 0.50 | 0.77 | 14 | empty |
| 4 | 92 | 0.46 | 0.80 | 15 | empty |
| 5 | 69 | 0.35 | 0.77 | 13 | 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 Q80TZ9
- Elsewhere: UniProt Q80TZ9 · AlphaFold DB Q80TZ9
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