EC Number   |
Subunits |
Reference |
|---|
   1.8.4.2 | dimer |
dimerization of COA6 is unaffected by its concentration. The residues in helix 3 of COA6 are likely involved in dimerization. Dimerization is not due to inter-disulfide bonding between cysteine residues of each COA6 monomer. COA6 structure analysis, overview |
-, 764441 |
| 1.8.4.2 | homodimer |
2 * 14000, SDS-PAGE |
-, 670797 |
| 1.8.4.2 | homodimer |
2 * 14056, unmodified recombinant WhiB1, MALDI-TOF mass spectrometry |
-, 670797 |
| 1.8.4.2 | homodimer |
2 * 14284, reduced protein after alkylation corresponding to the theoretical mass of the recombinant protein with four iodoacetamide mediated modifications of cysteines, MALDI-TOF mass spectrometry |
-, 670797 |
| 1.8.4.2 | monomer |
1 * 12000, SDS-PAGE |
763028 |
| 1.8.4.2 | monomer |
1 * 21100 |
394853 |
| 1.8.4.2 | monomer |
1 * 60000, SDS-PAGE |
394836 |
| 1.8.4.2 | monomer |
1 * 62500, SDS-PAGE |
394838 |
| 1.8.4.2 | More |
formation of an intramolecular disulfide between Cys27 and Cys30 within the CPYC active site of GRX2 |
763028 |
| 1.8.4.2 | More |
GRX5 can form covalent homodimers through intermolecular disulfide bonds |
763028 |
