Research workbench
AlphaFold monomer V2.0 prediction for dihydroxy-acid dehydratase (A9R8F3)
Analyse AlphaFold monomer V2.0 prediction for dihydroxy-acid dehydratase (A9R8F3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9R8F3
- Type
- protein
- Length
- 616 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x777B8f47014a4dE872e1b32733B9fD3c15840A7A
- Molecule
- Dihydroxy-acid dehydratase
- UniProt
- A9R8F3
- Pockets
- 5 · best druggability 0.62
Structure
1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroxy-acid dehydratase | protein | 616 | 42% helix, 15% strand | A9R8F3 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.62 | 0.83 | 46 | empty |
| 2 | 94 | 0.37 | 0.75 | 13 | empty |
| 3 | 79 | 0.35 | 0.76 | 20 | empty |
| 4 | 58 | 0.31 | 0.75 | 13 | empty |
| 5 | 78 | 0.29 | 0.72 | 16 | 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 A9R8F3
- Elsewhere: UniProt A9R8F3 · AlphaFold DB A9R8F3
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