Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase (Q88ZA0)
Analyse AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase (Q88ZA0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q88ZA0
- Type
- protein
- Length
- 234 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xCe798D8eC2d4C6C1A5c2B7B7212A387006233F43
- Molecule
- NAD-dependent protein deacetylase
- UniProt
- Q88ZA0
- Pockets
- 1 · best druggability 0.71
Structure
1 distinct chain · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacetylase | protein | 234 | 35% helix, 19% strand | Q88ZA0 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 307 | 0.71 | 0.85 | 45 | 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 Q88ZA0
- Elsewhere: UniProt Q88ZA0 · AlphaFold DB Q88ZA0
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