EC Number   |
Subunits |
Reference |
|---|
    2.9.1.1 | homodecamer |
- |
725024 |
| 2.9.1.1 | homodecamer |
10 * 50000, SDS-PAGE |
739586 |
| 2.9.1.1 | tetramer |
4 * 49000, SDS-PAGE |
693212 |
| 2.9.1.1 | More |
formation of the ternary enzyme complex and binding to the ribosome, structure analysis by electron microscopy, 5fold rotational symmetry, overview |
691146 |
| 2.9.1.1 | decamer |
the homodecamer has a ring-like structure with five bilobed wings, similar to the structure of the Escherichia coli complex |
691146 |
| 2.9.1.1 | More |
two SecS monomers interact intimately and together build up two identical active sites around PLP in a Schiff-base linkage with Lys284. Two SecS dimers further associate to form a homotetramer. The N-terminus, which mediates tetramer formation, and a large insertion that remodels the active site set SecS aside from other members of the family |
693212 |
| 2.9.1.1 | ? |
x * 48000, SDS-PAGE |
691179 |
| 2.9.1.1 | ? |
x * 50667, calculation from nucleotide sequence |
22913 |
| 2.9.1.1 | homodecamer |
x-ray crystallography |
739706 |
