EC Number |
Subunits |
Reference |
---|
1.14.11.1 | ? |
x * 42000, amino acid composition |
439298 |
1.14.11.1 | ? |
x * 44000, SDS-PAGE |
439300 |
1.14.11.1 | dimer |
- |
439298, 764457 |
1.14.11.1 | dimer |
1 * 39000 + 1 * 37000, SDS-PAGE, amino acid analysis, N-terminal amino acid sequence |
-, 439284 |
1.14.11.1 | dimer |
2 * 42000, SDS-PAGE |
439286 |
1.14.11.1 | dimer |
2 * 43000, amino acid analysis, a chain of 383 amino acids and a truncated chain of 382 amino acids |
-, 439298 |
1.14.11.1 | dimer |
2 * 43000, SDS-PAGE |
439301 |
1.14.11.1 | dimer |
2 * 46000, SDS-PAGE |
439286 |
1.14.11.1 | dimer |
SDS-PAGE, same value for all three isozymes, dimeric combinations of two subunits |
439289 |
1.14.11.1 | dimer |
the GBBH monomer consists of a catalytic double-stranded beta-helix domain, and a smaller N-terminal domain, the N-terminal domain of GBBH has a similar fold to the DUF971 superfamily. GBBH is dimeric in its biological state. the dimerization interface of GBBH is very different from that of related enzymes, three-dimensional structure, overview |
711108 |