Research workbench
AlphaFold monomer V2.0 prediction for dihydroxy-acid dehydratase (Q04I44)
Analyse AlphaFold monomer V2.0 prediction for dihydroxy-acid dehydratase (Q04I44) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q04I44
- Type
- protein
- Length
- 567 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- Dihydroxy-acid dehydratase
- UniProt
- Q04I44
- Pockets
- 4 · best druggability 0.61
Structure
1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroxy-acid dehydratase | protein | 567 | 43% helix, 15% strand | Q04I44 |
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 | 137 | 0.61 | 0.85 | 35 | empty |
| 2 | 97 | 0.38 | 0.76 | 17 | empty |
| 3 | 52 | 0.31 | 0.77 | 14 | empty |
| 4 | 50 | 0.30 | 0.77 | 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 Q04I44
- Elsewhere: UniProt Q04I44 · AlphaFold DB Q04I44
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