Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase (P66815)
Analyse AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase (P66815) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P66815
- Type
- protein
- Length
- 243 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF7e50Fe2e6fcA90573918459ED90298F35ceaE3D
- Molecule
- NAD-dependent protein deacetylase
- UniProt
- P66815
- Pockets
- 2 · best druggability 0.78
Structure
1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacetylase | protein | 243 | 39% helix, 19% strand | P66815 |
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 | 381 | 0.78 | 0.87 | 49 | empty |
| 2 | 58 | 0.29 | 0.74 | 11 | 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 P66815
- Elsewhere: UniProt P66815 · AlphaFold DB P66815
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