Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase SIRT2 (Q9I7I7)
Analyse AlphaFold monomer V2.0 prediction for NAD-dependent protein deacetylase SIRT2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9I7I7
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- NAD-dependent protein deacetylase SIRT2
- UniProt
- Q9I7I7
- Pockets
- 4 · best druggability 0.69
Structure
1 distinct chain · 39% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacetylase SIRT2 | protein | 355 | 39% helix, 14% strand | Q9I7I7 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 257 | 0.69 | 0.85 | 41 | empty |
| 2 | 53 | 0.68 | 0.96 | 19 | empty |
| 3 | 136 | 0.41 | 0.75 | 26 | empty |
| 4 | 104 | 0.36 | 0.74 | 18 | 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 Q9I7I7
- Elsewhere: UniProt Q9I7I7 · AlphaFold DB Q9I7I7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.