Research workbench
AlphaFold monomer V2.0 prediction for erythroid transcription factor (P15976)
Analyse AlphaFold monomer V2.0 prediction for erythroid transcription factor (P15976) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P15976
- Type
- protein
- Length
- 413 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- UniProt
- P15976
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 413 | — | P15976 |
Compared structures
- 6G0Q · Crystal structure of the first bromodomain of human BRD4 in complex with an acetylated… · an experimental structure of the same protein · chain A against B, TM-score 0.02
- 6G0Q · Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated… · an experimental structure of the same protein · chain A against B, TM-score 0.02
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 P15976
- Elsewhere: UniProt P15976 · AlphaFold DB P15976
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