Research workbench
AlphaFold monomer V2.0 prediction for histone chaperone ASF1 (Q4WXX5)
Analyse AlphaFold monomer V2.0 prediction for histone chaperone ASF1 (Q4WXX5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4WXX5
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x04Abc94644f002885c8999456744b144a9092D1d
- UniProt
- Q4WXX5
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 282 | — | Q4WXX5 |
Compared structures
- 5ZBB · Crystal structure of RTT109-ASF1-H3-H4 complex · an experimental structure of the same protein · chain A against B, TM-score 0.54
- 5ZBB · Crystal structure of Rtt109-Asf1-H3-H4 complex · an experimental structure of the same protein · chain A against B, TM-score 0.54
- 5ZBA · Crystal structure of RTT109-ASF1-H3-H4-CoA complex · an experimental structure of the same protein · chain A against B, TM-score 0.54
- 5ZBA · Crystal structure of Rtt109-Asf1-H3-H4-CoA complex · an experimental structure of the same protein · chain A against B, TM-score 0.54
- 7XAY · Crystal structure of HAT1-HAT2-ASF1-H3-H4 · an experimental structure of the same protein · chain A against C, TM-score 0.54
- 7XAY · Crystal structure of Hat1-Hat2-Asf1-H3-H4 · an experimental structure of the same protein · chain A against C, TM-score 0.54
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 Q4WXX5
- Elsewhere: UniProt Q4WXX5 · AlphaFold DB Q4WXX5
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