Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase sirtuin-2 (Q5RBF1)
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
- Q5RBF1
- Type
- protein
- Length
- 352 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
- Molecule
- NAD-dependent protein deacetylase sirtuin-2
- UniProt
- Q5RBF1
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 37% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacetylase sirtuin-2 | protein | 352 | 37% helix, 14% strand | Q5RBF1 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 454 | 0.78 | 0.86 | 61 | empty |
| 2 | 125 | 0.41 | 0.76 | 27 | empty |
| 3 | 98 | 0.37 | 0.75 | 17 | empty |
| 4 | 61 | 0.30 | 0.75 | 19 | 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 Q5RBF1
- Elsewhere: UniProt Q5RBF1 · AlphaFold DB Q5RBF1
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