EC Number   |
Subunits |
Reference |
|---|
    4.3.3.7 | ? |
alpha,beta or alpha2beta |
33911 |
| 4.3.3.7 | ? |
x * 31000, SDS-PAGE |
664072 |
| 4.3.3.7 | ? |
x * 33000, SDS-PAGE |
-, 677349 |
| 4.3.3.7 | ? |
x * 34680, mass spectrometry |
728886 |
| 4.3.3.7 | dimer |
- |
730669 |
| 4.3.3.7 | dimer |
2 * 31000, calculated from sequence |
-, 704696 |
| 4.3.3.7 | dimer |
2 * 31000, SDS-PAGE, recombinant untagged recombinant enzyme |
-, 749225 |
| 4.3.3.7 | dimer |
2 * 33000, SDS-PAGE, recombinant His-tagged recombinant enzyme |
-, 749225 |
| 4.3.3.7 | dimer |
2 * 62400, mutant A204R, crystal structure |
713969 |
| 4.3.3.7 | dimer |
three-dimensional structure determination shows that DHDPS forms a homodimer which is stabilized by several hydrogen bonds and van der Waals forces at the interface, active site structure, overview. Each monomer is composed of two domains, the N-terminal domain consists of residues 1-224, and forms an 8-fold parallel alpha/beta barrel |
715195 |
