Research workbench
AlphaFold monomer V2.0 prediction for SWR1-complex protein 5 (P38326)
Analyse AlphaFold monomer V2.0 prediction for SWR1-complex protein 5 (P38326) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P38326
- Type
- protein
- Length
- 303 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- Molecule
- SWR1-complex protein 5
- UniProt
- P38326
Structure
1 distinct chain · 41% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SWR1-complex protein 5 | protein | 303 | 41% helix, 7% strand | P38326 |
Compared structures
- 8QZ0 · SWR1-hexasome-dimer complex · an experimental structure of the same protein · chain A against P, TM-score 0.20
- 8QYV · SWR1-hexasome complex · an experimental structure of the same protein · chain A against P, TM-score 0.17
- 6KBB · Role of the DEF/Y motif of SWC5 in histone H2A.Z deposition · an experimental structure of the same protein · chain A against F, TM-score 0.05
- 6KBB · Role of the DEF/Y motif of Swc5 in histone H2A.Z deposition · an experimental structure of the same protein · chain A against F, TM-score 0.05
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 P38326
- Elsewhere: UniProt P38326 · AlphaFold DB P38326
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