Research workbench
AlphaFold monomer V2.0 prediction for secoisolariciresinol dehydrogenase (Q94KL7)
Analyse AlphaFold monomer V2.0 prediction for secoisolariciresinol dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q94KL7
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- Secoisolariciresinol dehydrogenase
- UniProt
- Q94KL7
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Secoisolariciresinol dehydrogenase | protein | 277 | 52% helix, 14% strand | Q94KL7 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 491 | 0.73 | 0.82 | 50 | empty |
| 2 | 87 | 0.54 | 0.85 | 19 | empty |
| 3 | 50 | 0.30 | 0.77 | 12 | empty |
| 4 | 64 | 0.27 | 0.73 | 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 Q94KL7
- Elsewhere: UniProt Q94KL7 · AlphaFold DB Q94KL7
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