Research workbench
AlphaFold monomer V2.0 prediction for aldehyde dehydrogenase family 1 member A3 (Q9JHW9)
Analyse AlphaFold monomer V2.0 prediction for aldehyde dehydrogenase family 1 member A3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9JHW9
- Type
- protein
- Length
- 512 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Aldehyde dehydrogenase family 1 member A3
- UniProt
- Q9JHW9
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldehyde dehydrogenase family 1 member A3 | protein | 512 | 39% helix, 20% strand | Q9JHW9 |
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 | 560 | 0.70 | 0.78 | 65 | empty |
| 2 | 96 | 0.35 | 0.75 | 14 | empty |
| 3 | 60 | 0.32 | 0.76 | 15 | 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 Q9JHW9
- Elsewhere: UniProt Q9JHW9 · AlphaFold DB Q9JHW9
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