CATH Domain 2q80A00

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	Geranylgeranyl pyrophosphate synthase

Enzyme Information

2.5.1.10	(2E,6E)-farnesyl diphosphate synthase. based on mapping to UniProt O95749 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.
2.5.1.29	Geranylgeranyl diphosphate synthase. based on mapping to UniProt O95749 (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate. -!- Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors.
2.5.1.1	Dimethylallyltranstransferase. based on mapping to UniProt O95749 Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate. -!- Will not accept larger prenyl diphosphates as efficient donors.
2.5.1.-	Transferring alkyl or aryl groups, other than methyl groups. based on mapping to UniProt O95749

UniProtKB Entries (1)

GGPPS_HUMAN

Homo sapiens

Geranylgeranyl pyrophosphate synthase

PDB Structure

PDB	2Q80
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	The crystal structure of human geranylgeranyl pyrophosphate synthase reveals a novel hexameric arrangement and inhibitory product binding Kavanagh, K.L., Dunford, J.E., Bunkoczi, G., Russell, R.G., Oppermann, U. J.Biol.Chem.