Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase (B5YJW3)
Analyse AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase (B5YJW3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5YJW3
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80c65687F966a6264124948aC6721671E4B4d776
- Molecule
- NAD-dependent protein deacetylase
- UniProt
- B5YJW3
- Pockets
- 2 · best druggability 0.79
Structure
1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacetylase | protein | 256 | 45% helix, 17% strand | B5YJW3 |
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 | 330 | 0.79 | 0.89 | 56 | empty |
| 2 | 65 | 0.34 | 0.76 | 13 | 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 B5YJW3
- Elsewhere: UniProt B5YJW3 · AlphaFold DB B5YJW3
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