EC Number |
Subunits |
Reference |
---|
2.7.7.23 | trimer |
crystal structure analysis |
643073 |
2.7.7.23 | trimer |
GlmU forms a biological trimer, and two independent domains in each monomer catalyze two independent reactions in the protein |
740866 |
2.7.7.23 | trimer |
the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein |
-, 729696 |
2.7.7.23 | trimer |
trimer/hexamer equilibrium, sedimentation equilibrium analytical ultracentrifugation. Two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction |
723724 |
2.7.7.23 | trimer |
two-domain architecture of GlmU, one monomer per asymmetric unit, and a trimeric quaternary structure known for GlmU proteins |
720042 |
2.7.7.23 | trimer |
x-ray crystallography |
-, 690292 |