EC Number   |
Subunits |
Reference |
|---|
    2.4.2.17 | hexamer |
inactive form, in complex with histidine |
637675 |
| 2.4.2.17 | homodimer |
2 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000 |
721765 |
| 2.4.2.17 | homohexamer |
6 * 31515.1, ESI-MS, gel filtration, His-tagged protein, not influenced by allosteric inhibitor L-histidine or ATP |
-, 721673 |
| 2.4.2.17 | homohexamer |
6 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000 |
721765 |
| 2.4.2.17 | homohexamer |
long enzyme form |
-, 758757 |
| 2.4.2.17 | homohexamer |
x-ray crystallography |
758758 |
| 2.4.2.17 | homohexamer or heterooctamer |
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine |
-, 758560 |
| 2.4.2.17 | More |
overall structure and monomer architecture, several motif 2 loops in both subunit types, switch structure between active and inactive conformation |
659495 |
| 2.4.2.17 | More |
quarternary structure |
659707 |
| 2.4.2.17 | More |
subunit structures, structure evolution |
659965 |
