Research workbench
AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT8 (Q9D1P2)
Analyse AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT8 (Q9D1P2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9D1P2
- Type
- protein
- Length
- 458 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- UniProt
- Q9D1P2
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 458 | — | Q9D1P2 |
Compared structures
- 1WGS · Solution Structure of the Tudor Domain from Mouse Hypothetical Protein Homologous to… · an experimental structure of the same protein · chain A against A, TM-score 0.15
- 1WGS · Solution structure of the tudor domain from mouse hypothetical protein homologous to… · an experimental structure of the same protein · chain A against A, TM-score 0.15
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 Q9D1P2
- Elsewhere: UniProt Q9D1P2 · AlphaFold DB Q9D1P2
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