Crystallization (Comment) | Organism |
---|---|
the structure of UGDH in the crystal form reveals a hexameric arrangement, composed a trimer of dimers of six subunits | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
A222Q/S233G | is a dimer in solution | Homo sapiens |
C276A | is a hexamer-dimer mixture | Homo sapiens |
C276S | is a hexamer | Homo sapiens |
D280N | shows, exclusively, a hexameric quaternary structure in solution | Homo sapiens |
K220A | shows, exclusively, a hexameric quaternary structure in solution | Homo sapiens |
K279A | is essentially a dimer | Homo sapiens |
K339A | is a dimer | Homo sapiens |
additional information | perturbation caused by the mutation of a residue at a considerably distant location from the oligomeric interfaces is preferentially distributed throughout specific sites, especially the large flexible regions in the hUGDH structure, thereby changing the motional fluctuation pattern at the oligomeric interfaces. A large-magnitude cooperative motion at the oligomeric interfaces is a critical factor in interfering with the hexamer formation of the enzyme. Structural stability at the dimeric interface is necessary to retain the hexameric structure of UGDH | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O60701 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
UDP-glucose dehydrogenase | - |
Homo sapiens |
UGDH | - |
Homo sapiens |