1BIF
6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE BIFUNCTIONAL ENZYME COMPLEXED WITH ATP-G-S AND PHOSPHATE
Summary for 1BIF
Entry DOI | 10.2210/pdb1bif/pdb |
NMR Information | BMRB: 5935 |
Descriptor | 6-PHOSPHOFRUCTO-2-KINASE/ FRUCTOSE-2,6-BISPHOSPHATASE, MAGNESIUM ION, PHOSPHATE ION, ... (6 entities in total) |
Functional Keywords | kinase, transferase (phospho), phosphatase, hydrolase (phospho), glycolysis, bifunctional enzyme |
Biological source | Rattus norvegicus (Norway rat) |
Total number of polymer chains | 1 |
Total formula weight | 54898.17 |
Authors | Hasemann, C.A.,Deisenhofer, J. (deposition date: 1996-11-08, release date: 1997-11-12, Last modification date: 2024-02-07) |
Primary citation | Hasemann, C.A.,Istvan, E.S.,Uyeda, K.,Deisenhofer, J. The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies. Structure, 4:1017-1029, 1996 Cited by PubMed Abstract: Glucose homeostasis is maintained by the processes of glycolysis and gluconeogenesis. The importance of these pathways is demonstrated by the severe and life threatening effects observed in various forms of diabetes. The bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. Thus this bifunctional enzyme plays an indirect yet key role in the regulation of glucose metabolism. PubMed: 8805587DOI: 10.1016/S0969-2126(96)00109-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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