Research workbench
AlphaFold monomer V2.0 prediction for bifunctional protein fold (Q99YX2)
Analyse AlphaFold monomer V2.0 prediction for bifunctional protein fold (Q99YX2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q99YX2
- Type
- protein
- Length
- 284 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa290d73B7A96341BDEd15630a89ebdADF7F8CE86
- Molecule
- Bifunctional protein fold
- UniProt
- Q99YX2
- Pockets
- 4 · best druggability 0.60
Structure
1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein fold | protein | 284 | 42% helix, 17% strand | Q99YX2 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 306 | 0.60 | 0.78 | 42 | empty |
| 2 | 159 | 0.42 | 0.74 | 28 | empty |
| 3 | 59 | 0.31 | 0.76 | 13 | empty |
| 4 | 61 | 0.29 | 0.74 | 10 | 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 Q99YX2
- Elsewhere: UniProt Q99YX2 · AlphaFold DB Q99YX2
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