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1TIP

THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE

Summary for 1TIP
Entry DOI10.2210/pdb1tip/pdb
NMR InformationBMRB: 5935
DescriptorPHOSPHOENZYME INTERMEDIATE OF FRU-2,6-BISPHOSPHATASE, 6-O-phosphono-beta-D-fructofuranose (3 entities in total)
Functional Keywordsmultifunctional enzyme, transferase, kinase, atp-binding, phosphorylation, alternative splicing, multigene family, hydrolase
Biological sourceRattus norvegicus (Norway rat)
Total number of polymer chains2
Total formula weight45036.94
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 citationLee, 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: 9253407
DOI: 10.1038/nsb0897-615
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

237735

数据于2025-06-18公开中

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