Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase (Q8PDM9)
Analyse AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase (Q8PDM9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8PDM9
- Type
- protein
- Length
- 293 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x934953E3d9faD9B1cC752f4A28d5f4E6903eA0Ce
- Molecule
- NAD-dependent protein deacetylase
- UniProt
- Q8PDM9
- Pockets
- 2 · best druggability 0.77
Structure
1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacetylase | protein | 293 | 40% helix, 18% strand | Q8PDM9 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 436 | 0.77 | 0.86 | 61 | empty |
| 2 | 131 | 0.42 | 0.76 | 23 | 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 Q8PDM9
- Elsewhere: UniProt Q8PDM9 · AlphaFold DB Q8PDM9
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