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AlphaFold monomer V2.0 prediction for short chain DEHYDROGENASE/REDUCTASE dpchh (A0A1B7YCL6)
Analyse AlphaFold monomer V2.0 prediction for short chain DEHYDROGENASE/REDUCTASE dpchh… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A1B7YCL6
- Type
- protein
- Length
- 401 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7A237143798c68038d48886A489bD0505943F92E
- Molecule
- Short chain DEHYDROGENASE/REDUCTASE dpchh
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Short chain DEHYDROGENASE/REDUCTASE dpchh | protein | 401 | 52% helix, 10% strand | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 564 | 0.67 | 0.77 | 49 | empty |
| 2 | 278 | 0.54 | 0.76 | 26 | empty |
| 3 | 50 | 0.27 | 0.75 | 17 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
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