Research workbench
AlphaFold monomer V2.0 prediction for dihydroxy-acid dehydratase (A5GTE2)
Analyse AlphaFold monomer V2.0 prediction for dihydroxy-acid dehydratase (A5GTE2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5GTE2
- Type
- protein
- Length
- 558 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Dihydroxy-acid dehydratase
- UniProt
- A5GTE2
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroxy-acid dehydratase | protein | 558 | 41% helix, 16% strand | A5GTE2 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.69 | 0.96 | 23 | empty |
| 2 | 119 | 0.45 | 0.77 | 28 | empty |
| 3 | 91 | 0.35 | 0.74 | 17 | 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 A5GTE2
- Elsewhere: UniProt A5GTE2 · AlphaFold DB A5GTE2
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