Research workbench
AlphaFold monomer V2.0 prediction for transcription factor hes-1 (Q14469)
Analyse AlphaFold monomer V2.0 prediction for transcription factor hes-1 (Q14469) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q14469
- Type
- protein
- Length
- 280 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- UniProt
- Q14469
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 280 | — | Q14469 |
Compared structures
- 2MH3 · NMR structure of the basic helix-loop-helix region of the transcriptional repressor hes-1 · an experimental structure of the same protein · chain A against A, TM-score 0.20
- 2MH3 · NMR structure of the basic helix-loop-helix region of the transcriptional repressor HES-1 · an experimental structure of the same protein · chain A against A, TM-score 0.20
- 7C4O · Solution structure of the orange domain from human protein HES1 · an experimental structure of the same protein · chain A against B, TM-score 0.16
- 7C4O · Solution structure of the Orange domain from human protein HES1 · an experimental structure of the same protein · chain A against B, TM-score 0.16
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 Q14469
- Elsewhere: UniProt Q14469 · AlphaFold DB Q14469
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