Research workbench
AlphaFold monomer V2.0 prediction for histone acetyltransferase GCN5 (Q6CXW4)
Analyse AlphaFold monomer V2.0 prediction for histone acetyltransferase GCN5 (Q6CXW4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6CXW4
- Type
- protein
- Length
- 516 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe340A9B41D01C54a08445aF15bF7964694Ad25cd
- Molecule
- Histone acetyltransferase GCN5
- UniProt
- Q6CXW4
- Pockets
- 3 · best druggability 0.61
Structure
1 distinct chain · 35% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase GCN5 | protein | 516 | 35% helix, 11% strand | Q6CXW4 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.61 | 0.78 | 40 | empty |
| 2 | 281 | 0.56 | 0.76 | 39 | empty |
| 3 | 142 | 0.44 | 0.76 | 27 | 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 Q6CXW4
- Elsewhere: UniProt Q6CXW4 · AlphaFold DB Q6CXW4
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