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 | 4PVY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystallographic and thermodynamic characterization of phenylaminopyridine bisphosphonates binding to human farnesyl pyrophosphate synthase.
PLoS ONE
|
