Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent histone deacetylase SIR2 (Q6FWI7)
Analyse AlphaFold monomer V2.0 prediction for NAD-dependent histone deacetylase SIR2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6FWI7
- Type
- protein
- Length
- 509 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA777E42419704A95462d8413746e87F7381Bd58e
- Molecule
- NAD-dependent histone deacetylase SIR2
- UniProt
- Q6FWI7
- Pockets
- 8 · best druggability 0.71
Structure
1 distinct chain · 37% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent histone deacetylase SIR2 | protein | 509 | 37% helix, 13% strand | Q6FWI7 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.71 | 0.84 | 51 | empty |
| 2 | 626 | 0.67 | 0.76 | 61 | empty |
| 3 | 448 | 0.64 | 0.77 | 40 | empty |
| 4 | 68 | 0.61 | 0.90 | 16 | empty |
| 5 | 298 | 0.55 | 0.76 | 28 | 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 Q6FWI7
- Elsewhere: UniProt Q6FWI7 · AlphaFold DB Q6FWI7
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