EC 1.1.1.251: galactitol-1-phosphate 5-dehydrogenase
This is an abbreviated version!
For detailed information about galactitol-1-phosphate 5-dehydrogenase, go to the full flat file.
Reaction
Synonyms
galactitol-1-phosphate dehydrogenase (Escherichia coli strain EC3132 gene gatD), Gat1P-specific NAD-dependent dehydrogenase, GatD, Genbank X79837-derived protein, GPDH, NAD-dependent Gat1P-dehydrogenase
ECTree
1.1.1.251 galactitol-1-phosphate 5-dehydrogenaseAdvanced search results
results (
results (| Results | in table |
|---|---|
| 92 | AA Sequence |
| 2 | CAS Registry Number |
| 1 | Cloned(Commentary) |
| 1 | Cofactor |
| 2 | Crystallization (Commentary) |
| 1 | Metals/Ions |
| 2 | Molecular Weight [Da] |
| 2 | Natural Substrates/ Products (Substrates) |
| 7 | Organism |
| 4 | Pathway |
| 8 | PDB ID |
| 1 | Reaction |
| 2 | Reaction Type |
| 7 | Reference |
| 6 | Substrates and Products (Substrate) |
| 4 | Subunits |
| 8 | Synonyms |
| 1 | Systematic Name |
Crystallization
Crystallization on EC 1.1.1.251 - galactitol-1-phosphate 5-dehydrogenase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
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
structures of open state with Zn2+ in the catalytic site and of the closed state in complex with the polyols Tris and glycerol, respectively. The closed state reveals no bound cofactor. The glycerol binding mode reveals a pentacoordinated zinc ion in complex with a polyol and also a strong hydrogen bond between the primary hydroxyl group and the conserved Glu144
