Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent protein deacylase (Q8Y015)
Analyse AlphaFold monomer V2.0 prediction for NAD-dependent protein deacylase (Q8Y015) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8Y015
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD19Af9471eB6CA1bcfd4838F07B82c3d9E99d50A
- Molecule
- NAD-dependent protein deacylase
- UniProt
- Q8Y015
- Pockets
- 1 · best druggability 0.75
Structure
1 distinct chain · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacylase | protein | 246 | 38% helix, 19% strand | Q8Y015 |
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 | 374 | 0.75 | 0.85 | 55 | 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 Q8Y015
- Elsewhere: UniProt Q8Y015 · AlphaFold DB Q8Y015
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