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MMDB ID: 57444
PDB ID: 1TDJ
Reference: Gallagher DT, Gilliland GL, Xiao G, Zondlo J, Fisher KE, Chinchilla D, Eisenstein EStructure and control of pyridoxal phosphate dependent allosteric threonine deaminaseStructure v6, p.465-475
BACKGROUND: Feedback inhibition of biosynthetic threonine deaminase (TD) from Escherichia coli provided one of the earliest examples of protein-based metabolic regulation. Isoleucine, the pathway end-product, and valine, the product of a parallel pathway, serve as allosteric inhibitor and activator, respectively. This enzyme is thus a useful model system for studying the structural basis of allosteric control mechanisms....
Description: Threonine Deaminase (Biosynthetic) From E. Coli.
Deposition: 1998/3/27 Click for more information 
Taxonomy: Escherichia coli
Related Structure: VAST
Molecular components in the MMDB structure are listed below and may include macromolecular chains, 3D domains, protein classifications (domain families), and ligands, as available. Mouse over each icon for more information on the component.Click to see help




 

 

Ligand
Synonyms: Pyridoxamine-P,pyridoxamine phosphate,Pyridoxamine 5-phosphate,pyridoxamine 5'-phosphate,PYRIDOXAMINE-5'-PHOSPHATE,1zc9,Pyridoxamine phosphate [JAN],bmse000131,Pyridoxamine, dihydrogen phosphate,UNII-Q05R77UO7P,951-83-7 (hydrochloride),82890_FLUKA,82890_SIGMA,CHEBI:18335,EINECS 208-471-6,Pyridoxamine, 3-(dihydrogen phosphate)... -Click for PubChem compound information Zoom the image
pyridoxamine ph..
 
1 occurrence
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