Research workbench
AlphaFold monomer V2.0 prediction for protein ydep (Q83RF3)
Analyse AlphaFold monomer V2.0 prediction for protein ydep (Q83RF3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q83RF3
- Type
- protein
- Length
- 759 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3e8e3909a877B69b46206B47B350b98db3C5644b
- Molecule
- Protein ydep
- UniProt
- Q83RF3
- Pockets
- 8 · best druggability 0.88
Structure
1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein ydep | protein | 759 | 39% helix, 19% strand | Q83RF3 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 461 | 0.88 | 0.96 | 85 | empty |
| 2 | 501 | 0.65 | 0.77 | 39 | empty |
| 3 | 171 | 0.59 | 0.82 | 28 | empty |
| 4 | 266 | 0.59 | 0.79 | 47 | empty |
| 5 | 163 | 0.55 | 0.80 | 25 | 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 Q83RF3
- Elsewhere: UniProt Q83RF3 · AlphaFold DB Q83RF3
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