Research workbench
AlphaFold monomer V2.0 prediction for ets translocation variant 4 (P43268)
Analyse AlphaFold monomer V2.0 prediction for ets translocation variant 4 (P43268) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P43268
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd1A2963012bEcbC7A8f505464439Ab678C48936f
- UniProt
- P43268
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 484 | — | P43268 |
Compared structures
- 4CO8 · Structure of the DNA binding ets domain of human ETV4 · an experimental structure of the same protein · chain A against A, TM-score 0.20
- 4CO8 · Structure of the DNA binding ETS domain of human ETV4 · an experimental structure of the same protein · chain A against A, TM-score 0.20
- 5ILU · Autoinhibited ETV4 · an experimental structure of the same protein · chain A against A, TM-score 0.20
- 5ILU · Autoinhibited ETV4 · an experimental structure of the same protein · chain A against A, TM-score 0.20
- 4UUV · Structure of the DNA binding ETS domain of human ETV4 in complex with DNA · an experimental structure of the same protein · chain A against P, TM-score 0.20
- 4UUV · Structure of the DNA binding ets domain of human ETV4 in complex with DNA · an experimental structure of the same protein · chain A against P, TM-score 0.20
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 P43268
- Elsewhere: UniProt P43268 · AlphaFold DB P43268
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