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Literature summary for 4.2.1.96 extracted from
- Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2 (2004), Biochemistry, 43, 7345-7355.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging-drop vapor diffusion method at 4°C, 1.6 A resolution crystal structure, space group P3(1)21, unit cell length: a = b = 57.92 A, c = 114.63 A | Mus musculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | Q9CZL5 | DcoH2 (dimerization cofactor of HNF1alpha) | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| DcoH2 (dimerization cofactor of HNF1alpha) | Mus musculus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | DcoH2 (dimerization cofactor of HNF1alpha), forms a tetramer, readily disproportionates and forms a 2:2 complex with HNF1 in vitro | Mus musculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DcoH2 | dimerization cofactor of HNF1alpha | Mus musculus |
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