Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase sirtuin-2 (Q4R834)
Analyse AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4R834
- Type
- protein
- Length
- 389 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- NAD-dependent protein deacetylase sirtuin-2
- UniProt
- Q4R834
- Pockets
- 5 · best druggability 0.79
Structure
1 distinct chain · 35% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacetylase sirtuin-2 | protein | 389 | 35% helix, 13% strand | Q4R834 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 368 | 0.79 | 0.88 | 54 | empty |
| 2 | 127 | 0.40 | 0.75 | 21 | empty |
| 3 | 128 | 0.39 | 0.74 | 27 | empty |
| 4 | 72 | 0.33 | 0.76 | 17 | empty |
| 5 | 64 | 0.31 | 0.74 | 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 Q4R834
- Elsewhere: UniProt Q4R834 · AlphaFold DB Q4R834
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