CATH Classification

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.
Park, J., Lin, Y.S., De Schutter, J.W., Tsantrizos, Y.S., Berghuis, A.M.
Bmc Struct.Biol.