EC Number   |
Subunits |
Reference |
|---|
   3.1.8.2 | monomer |
1 * 53000 SDS-PAGE |
646548 |
| 3.1.8.2 | monomer |
1 * 60000, SDS-PAGE, under reducing and nonreducing conditions |
646547 |
| 3.1.8.2 | homodimer |
2 * 35000, OPH from displays the TIM barrel fold in the active site loaded with Zn2+, overview |
713896 |
| 3.1.8.2 | tetramer |
active enzyme |
713896 |
| 3.1.8.2 | tetramer |
active enzyme, OPAA/prolidase from Alteromonas sp. JD6.5 displays the pita bread fold in the C-terminal region which houses the active metal site loaded with Mn2+, overview |
-, 713896 |
| 3.1.8.2 | More |
features observed in the structure of PON1, i.e. the six-bladed beta-propeller scaffold, the three alpha-helices at the top of the propeller and the putative calcium-binding residues, are well conserved in the modelled structures |
749628 |
| 3.1.8.2 | More |
the molecular conformation of DFPase is similar to other phosphotriesterases such as paraoxonase 1 (PON1, EC 3.1.8.1) |
750923 |
| 3.1.8.2 | ? |
x * 34000, SDS-PAGE |
664937 |
| 3.1.8.2 | ? |
x * 34000, SMP30, SDS-PAGE |
664937 |
| 3.1.8.2 | ? |
x * 35000 |
713615 |
