MolNFT v1 · #163227 · protein
AlphaFold monomer V2.0 prediction for histone H2AX (P16104)
P16104: “AlphaFold monomer V2.0 prediction for histone H2AX (P16104)”. MolNFT v1 #163227 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P16104
- Type
- protein
- Length
- 143 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- UniProt
- P16104
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 143 | — | P16104 |
Compared structures
- 6K1K · Human nucleosome core particle with H2A.X S139E variant · an experimental structure of the same protein · chain A against G, TM-score 0.77
- 6K1K · Human nucleosome core particle with H2A.X S139E variant · an experimental structure of the same protein · chain A against G, TM-score 0.77
- 6K1J · Human nucleosome core particle with H2A.X variant · an experimental structure of the same protein · chain A against G, TM-score 0.75
- 6K1I · Human nucleosome core particle with GAMMAH2A.X variant · an experimental structure of the same protein · chain A against C, TM-score 0.74
- 2DYP · Crystal structure of LILRB2(LIR2/ILT4/CD85D) complexed with HLA-G · an experimental structure of the same protein · chain A against C, TM-score 0.06
- 2DYP · Crystal Structure of LILRB2(LIR2/ILT4/CD85d) complexed with HLA-G · an experimental structure of the same protein · chain A against C, TM-score 0.06
- 2D31 · Crystal structure of disulfide-linked HLA-G dimer · an experimental structure of the same protein · chain A against C, TM-score 0.06
- 2D31 · Crystal structure of disulfide-linked HLA-G dimer · an experimental structure of the same protein · chain A against C, TM-score 0.06
- 6ZWK · Crystal structure of the phosphorylated C-terminal tail of histone H2AX in complex with a… · an experimental structure of the same protein · chain A against J, 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 P16104
- Elsewhere: UniProt P16104 · AlphaFold DB P16104
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