Research workbench
AlphaFold monomer V2.0 prediction for retinol dehydrogenase 10 (Q8VCH7)
Analyse AlphaFold monomer V2.0 prediction for retinol dehydrogenase 10 (Q8VCH7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8VCH7
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71112d4fF7ebb3b617963c05f052289e073082FD
- Molecule
- Retinol dehydrogenase 10
- UniProt
- Q8VCH7
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 57% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinol dehydrogenase 10 | protein | 341 | 57% helix, 12% strand | Q8VCH7 |
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 | 213 | 0.71 | 0.87 | 30 | empty |
| 2 | 286 | 0.64 | 0.81 | 43 | empty |
| 3 | 100 | 0.37 | 0.75 | 17 | empty |
| 4 | 66 | 0.30 | 0.74 | 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 Q8VCH7
- Elsewhere: UniProt Q8VCH7 · AlphaFold DB Q8VCH7
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