MolNFT v1 · #163920 · protein
AlphaFold monomer V2.0 prediction for histone H4 (P02309)
P02309: “AlphaFold monomer V2.0 prediction for histone H4 (P02309)”. MolNFT v1 #163920 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P02309
- Type
- protein
- Length
- 103 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x56320e99dA0e57c407C71A99Fa809492Af193C13
- UniProt
- P02309
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 103 | — | P02309 |
Compared structures
- 4JJN · Crystal structure of heterochromatin protein SIR3 in complex with a silenced yeast… · an experimental structure of the same protein · chain A against B, TM-score 0.76
- 4JJN · Crystal structure of heterochromatin protein Sir3 in complex with a silenced yeast… · an experimental structure of the same protein · chain A against B, TM-score 0.76
- 4KUD · Crystal structure of N-terminal acetylated Sir3 BAH domain D205N mutant in complex with… · an experimental structure of the same protein · chain A against F, TM-score 0.76
- 4KUD · Crystal structure of N-terminal acetylated SIR3 bah domain D205N mutant in complex with… · an experimental structure of the same protein · chain A against F, TM-score 0.76
- 6GEJ · Chromatin remodeller-nucleosome complex at 3.6 A resolution. · an experimental structure of the same protein · chain A against C, TM-score 0.75
- 6GEJ · Chromatin remodeller-nucleosome complex at 3.6 a resolution. · an experimental structure of the same protein · chain A against C, TM-score 0.75
- 7E9F · Cryo-EM structure of the 2:1 Orc1 BAH domain in complex with nucleosome · an experimental structure of the same protein · chain A against B, TM-score 0.75
- 8QKU · SWR1-nucleosome complex in configuration 1 · an experimental structure of the same protein · chain A against C, TM-score 0.75
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 P02309
- Elsewhere: UniProt P02309 · AlphaFold DB P02309
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