Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent protein deacylase SIR2 (A0R2N3)
Analyse AlphaFold monomer V2.0 prediction for NAD-dependent protein deacylase SIR2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0R2N3
- Type
- protein
- Length
- 240 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xccb8A171172ee5a65301D5F34Eef7EA7D46093B4
- Molecule
- NAD-dependent protein deacylase SIR2
- UniProt
- A0R2N3
- Pockets
- 1 · best druggability 0.79
Structure
1 distinct chain · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacylase SIR2 | protein | 240 | 36% helix, 19% strand | A0R2N3 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 407 | 0.79 | 0.88 | 56 | 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 A0R2N3
- Elsewhere: UniProt A0R2N3 · AlphaFold DB A0R2N3
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