EC Number   |
Subunits |
Reference |
|---|
    5.4.3.8 | dimer |
- |
3432, 727125 |
| 5.4.3.8 | monomer |
1 * 43000, SDS-PAGE |
3436 |
| 5.4.3.8 | dimer |
2 * 45000, SDS-PAGE |
3438 |
| 5.4.3.8 | dimer |
2 * 45500, SDS-PAGE, native and recombinant GSA-AT |
653764 |
| 5.4.3.8 | dimer |
2 * 46000, SDS-PAGE |
3437 |
| 5.4.3.8 | dimer |
2 * 46172, calculation from nucleotide sequence |
3437 |
| 5.4.3.8 | dimer |
2 * 56000, SDS-PAGE |
-, 3440 |
| 5.4.3.8 | dimer |
enzyme AtGSA1 forms an asymmetric dimer and displays asymmetry in cofactor binding as well as in the gating-loop orientation |
746660 |
| 5.4.3.8 | More |
the overall structure of AtGSA1 consists of three sequentially arranged domains: the N-terminal domain (Val1-Asp63, mature protein) comprises one alpha-helix and a three-stranded antiparallel beta-sheet, the pyridoxamine 5'-phosphate/pyridoxal 5'-phosphate-binding domain (Tyr64-Gly328), which is also the catalytic domain, contains a central seven-stranded beta-sheet with one antiparallel and six parallel beta-strands, and the C-terminal domain (Thr329-Ile434) is composed of a three-stranded antiparallel beta-sheet with four helices covering the outer surface. Asymmetry of AtGSA1 in the gating-loop conformation, overview |
746660 |
| 5.4.3.8 | dimer |
three-dimensional structure analysis of wild-type and mutant enzymes, overview |
-, 747005 |
