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Literature summary for 1.1.1.251 extracted from
- Substrate and cofactor binding interaction studies of galactitol-1-phosphate 5-dehydrogenase from Peptoclostridium difficile (2016), J. Teknol., 78, 199-210.
No PubMed abstract available
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| modeling of structure and docking analysis of substrate, Zn2+ and NAD+. Cys 37, His 58, Glu 59, Glu 142 residues form an active site pocket similar to known GPDH. A catalytic Zn2+-binding domain and a cofactor NAD+-binding domain with strong hydrogen bonding contacts with the substrate and the cofactor are identified | Clostridioides difficile |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Clostridioides difficile | A0A0H3N4Z0 | - |
- |
| Clostridioides difficile CD196 | A0A0H3N4Z0 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GatD | - |
Clostridioides difficile |
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Release 2023.1 (January 2023)
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