CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 1 | Mainly Alpha | 
|   | 1.10 | Orthogonal Bundle | 
|   | 1.10.600 | Farnesyl Diphosphate Synthase | 
|   | 1.10.600.10 | Farnesyl Diphosphate Synthase | 
Domain Context
CATH Clusters
| Superfamily | Farnesyl Diphosphate Synthase | 
| Functional Family | Farnesyl pyrophosphate synthase | 
Enzyme Information
| 2.5.1.1 | Dimethylallyltranstransferase. based on mapping to UniProt P14324 Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate. -!- Will not accept larger prenyl diphosphates as efficient donors. | 
| 2.5.1.10 | (2E,6E)-farnesyl diphosphate synthase. based on mapping to UniProt P14324 Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)- farnesyl diphosphate. -!- Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate. -!- The enzyme will not accept larger prenyl diphosphates as efficient donors. | 
UniProtKB Entries (1)
| P14324 | FPPS_HUMAN Homo sapiens Farnesyl pyrophosphate synthase | 
PDB Structure
| PDB | 4DEM | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Design and Synthesis of Active Site Inhibitors of the Human Farnesyl Pyrophosphate Synthase: Apoptosis and Inhibition of ERK Phosphorylation in Multiple Myeloma Cells. J.Med.Chem. | 
