1TIP
THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE
Summary for 1TIP
Entry DOI | 10.2210/pdb1tip/pdb |
NMR Information | BMRB: 5935 |
Descriptor | PHOSPHOENZYME INTERMEDIATE OF FRU-2,6-BISPHOSPHATASE, 6-O-phosphono-beta-D-fructofuranose (3 entities in total) |
Functional Keywords | multifunctional enzyme, transferase, kinase, atp-binding, phosphorylation, alternative splicing, multigene family, hydrolase |
Biological source | Rattus norvegicus (Norway rat) |
Total number of polymer chains | 2 |
Total formula weight | 45036.94 |
Authors | Lee, Y.-H.,Olson, T.W.,Ogata, C.M.,Levitt, D.G.,Banaszak, L.J.,Lange, A.J. (deposition date: 1997-05-28, release date: 1998-01-28, Last modification date: 2025-03-26) |
Primary citation | Lee, Y.H.,Olson, T.W.,Ogata, C.M.,Levitt, D.G.,Banaszak, L.J.,Lange, A.J. Crystal structure of a trapped phosphoenzyme during a catalytic reaction. Nat.Struct.Biol., 4:615-618, 1997 Cited by PubMed Abstract: The crystal structure of the fructose-2,6-bisphosphatase domain trapped during the reaction reveal a phosphorylated His 258, and a water molecule immobilized by the product, fructose-6-phosphate. The geometry suggests that the dephosphorylation step requires prior removal of the product for an 'associative in-line' phosphoryl transfer to the catalytic water. PubMed: 9253407DOI: 10.1038/nsb0897-615 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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