EC Number   |
Subunits |
Reference |
|---|
   1.10.3.3 | dimer |
unfolding studies, pressure-induced and denaturing agents-induced dissociation and unfolding, and the role of dimerization in the folding strategy of a large protein, crystal structure analysis, physico-chemical properties of a molten dimer enzyme, three distinct domains per subunit, sharing a common beta-barrel topology, overview |
673569 |
| 1.10.3.3 | dodecamer |
12 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE |
439924 |
| 1.10.3.3 | heterodimer |
1 * 72000 + 1 * 75000 |
764566 |
| 1.10.3.3 | homodimer |
ascorbate oxidase is a large, multidomain, dimeric protein |
724962 |
| 1.10.3.3 | monomer |
1 * 30000, enzyme also exists as dimer and tetramer, SDS-PAGE |
439924 |
| 1.10.3.3 | monomer |
1 * 35000, enzyme also exists as tetramer, octamer, dodecamer and polymer, SDS-PAGE |
439924 |
| 1.10.3.3 | monomer |
1 * 80000 |
-, 439929 |
| 1.10.3.3 | More |
each subunit is devided into 3 domains |
439902 |
| 1.10.3.3 | More |
quarternary structure |
439925 |
| 1.10.3.3 | More |
structure analysis: the monomers keep their secondary structure, whereas subtle conformational changes in the tertiary structure become apparent, salt bridges and electrostatic interactions occurring at the dimeric interface play a crucial role in the stabilization of the monomer's tertiary structure., folding/unfolding pathway, overview. Each subunit is formed by three distinct domains and contains four copper ions, three of which are located at the interface between domains, forming a so-called trinuclear centre |
724962 |
