Research workbench
AlphaFold monomer V2.0 prediction for NAD-dependent protein deacylase (Q72RR0)
Analyse AlphaFold monomer V2.0 prediction for NAD-dependent protein deacylase (Q72RR0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q72RR0
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3e0aC98Dc58EA794394EdeA1992f0D3Ca753d03c
- Molecule
- NAD-dependent protein deacylase
- UniProt
- Q72RR0
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacylase | protein | 246 | 39% helix, 20% strand | Q72RR0 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 384 | 0.77 | 0.87 | 50 | empty |
| 2 | 81 | 0.37 | 0.77 | 22 | empty |
| 3 | 50 | 0.28 | 0.75 | 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 Q72RR0
- Elsewhere: UniProt Q72RR0 · AlphaFold DB Q72RR0
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