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 | 4H5D |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Ternary complex structures of human farnesyl pyrophosphate synthase bound with a novel inhibitor and secondary ligands provide insights into the molecular details of the enzyme's active site closure.
Bmc Struct.Biol.
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