Research workbench
AlphaFold monomer V2.0 prediction for histone deacetylase complex subunit SAP30L (Q5SQF8)
Analyse AlphaFold monomer V2.0 prediction for histone deacetylase complex subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5SQF8
- Type
- protein
- Length
- 182 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Histone deacetylase complex subunit SAP30L
- UniProt
- Q5SQF8
- Pockets
- 3 · best druggability 0.50
Structure
1 distinct chain · 34% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone deacetylase complex subunit SAP30L | protein | 182 | 34% helix, 8% strand | Q5SQF8 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.50 | 0.77 | 21 | empty |
| 2 | 79 | 0.36 | 0.76 | 21 | empty |
| 3 | 64 | 0.30 | 0.73 | 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 Q5SQF8
- Elsewhere: UniProt Q5SQF8 · AlphaFold DB Q5SQF8
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