Crystallization (Comment) | Organism |
---|---|
catalytic subunit CdtA in its native form at pH 4.0, 8.5, and 9.0 and in complex with ADP-ribose donors, NAD+ and NADPH at pH 9.0. The crystal structures of the native protein show pronounced conformational flexibility confined to the active site region of the protein and enhanced disorder at low pH. The suggested catalytically important residues Glu385 and Glu387 seem to play no role or a less important role in ligand binding | Clostridioides difficile |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridioides difficile | Q9KH42 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
ADP-ribosyltransferase enzymatic component | - |
Clostridioides difficile |
CdtA | - |
Clostridioides difficile |