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 4QXS
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Probing the molecular and structural elements of ligands binding to the active site versus an allosteric pocket of the human farnesyl pyrophosphate synthase.
Gritzalis, D., Park, J., Chiu, W., Cho, H., Lin, Y.S., De Schutter, J.W., Lacbay, C.M., Zielinski, M., Berghuis, A.M., Tsantrizos, Y.S.
Bioorg.Med.Chem.Lett.