EC Number |
Subunits |
Reference |
---|
4.1.1.11 | tetramer |
- |
728327 |
4.1.1.11 | monomer |
1 * 410000, SDS-PAGE |
744560 |
4.1.1.11 | tetramer |
4 * 14000 |
650836 |
4.1.1.11 | homotetramer |
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE |
650998 |
4.1.1.11 | tetramer |
4 * 16000, recombinant enzyme, inactive pi-proenzyme, which is cleaved into the 13.22 kDa alpha-subunit and 2.74 kDa beta-subunit, processing is not essential for tetramer formation, SDS-PAGE |
-, 653749 |
4.1.1.11 | tetramer |
active enzyme is a tetramer composed of three alpha- and beta-subunits and an incompletely processed pi-protein |
-, 649350 |
4.1.1.11 | tetramer |
crystallographic data. Tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each end. The active sites are located between adjacent subunits |
3949 |
4.1.1.11 | More |
proform enzyme structure homology modeling, overview |
-, 727234 |
4.1.1.11 | dimer |
recombinant GAD |
-, 748086 |
4.1.1.11 | tetramer |
the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit |
-, 749207 |