Research workbench
AlphaFold monomer V2.0 prediction for histone H2A-beta (P04910)
Analyse AlphaFold monomer V2.0 prediction for histone H2A-beta (P04910) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P04910
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x41f14059A2ce2B9bfD2DFE723f11dad3eCa2614e
- UniProt
- P04910
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 131 | — | P04910 |
Compared structures
- 7YBF · Crystal structure of inner membrane protein Sad1 in complex with histone H2A-H2B · an experimental structure of the same protein · chain A against B, TM-score 0.63
- 7P0L · Crystal structure of S.POMBE MDB1 brct domains in complex with a H2A phosphopeptide · an experimental structure of the same protein · chain A against C, TM-score 0.04
- 7P0L · Crystal structure of S.pombe Mdb1 BRCT domains in complex with a H2A phosphopeptide · an experimental structure of the same protein · chain A against C, TM-score 0.04
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 P04910
- Elsewhere: UniProt P04910 · AlphaFold DB P04910
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