3cp6
Crystal structure of human farnesyl diphosphate synthase (T201A mutant) complexed with Mg and biphosphonate inhibitorCrystal structure of human farnesyl diphosphate synthase (T201A mutant) complexed with Mg and biphosphonate inhibitor
Structural highlights
Function[FPPS_HUMAN] Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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OCACategories:
- Homo sapiens
- Arrowsmith, C H
- Barnett, B L
- Bountra, C
- Delft, F von
- Dunford, J E
- Ebetino, F H
- Edwards, A M
- Guo, K
- Oppermann, U
- Pike, A C.W
- Pilka, E S
- Russell, R G.G
- Structural genomic
- Bisphosphonate
- Cholesterol biosynthesis
- Cholesterol synthesis
- Host-virus interaction isoprene biosynthesis
- Isoprenoid pathway
- Lipid synthesis
- Sgc
- Steroid biosynthesis
- Sterol biosynthesis
- Transferase