2Z4V

S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium and GGPP (inhibitory site)

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Terpenoid synthases	8068358	3001615	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Terpenoid synthases	8068358	3001615	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	polyprenyl_synt	e2z4vA1	A: alpha bundles	X: Terpenoid synthases (From Topology)	H: Terpenoid synthases (From Topology)	T: Terpenoid synthases	F: polyprenyl_synt	ECOD (1.6)
B	polyprenyl_synt	e2z4vB1	A: alpha bundles	X: Terpenoid synthases (From Topology)	H: Terpenoid synthases (From Topology)	T: Terpenoid synthases	F: polyprenyl_synt	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.600.10	Mainly Alpha	Orthogonal Bundle	Farnesyl Diphosphate Synthase	Farnesyl Diphosphate Synthase	CATH (4.3.0)
B	1.10.600.10	Mainly Alpha	Orthogonal Bundle	Farnesyl Diphosphate Synthase	Farnesyl Diphosphate Synthase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00348	Polyprenyl synthetase (polyprenyl_synt)	Polyprenyl synthetase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Geranylgeranyl pyrophosphate synthetase	farnesyltranstransferase activity prenyltransferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity dimethylallyltranstransferase activity geranyltranstransferase activity cation binding ion binding binding metal ion binding small molecule binding	protein localization establishment of protein localization cellular localization nitrogen compound transport transport establishment of localization localization protein transport cellular macromolecule localization macromolecule localization cellular process biosynthetic process isoprenoid biosynthetic process lipid biosynthetic process protein localization establishment of protein localization cellular localization nitrogen compound transport transport establishment of localization localization protein transport cellular macromolecule localization macromolecule localization cellular process biosynthetic process isoprenoid biosynthetic process lipid biosynthetic process primary metabolic process metabolic process terpenoid biosynthetic process terpenoid metabolic process lipid metabolic process isoprenoid metabolic process phospholipid biosynthetic process farnesyl diphosphate metabolic process phospholipid metabolic process farnesyl diphosphate biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process phosphorus metabolic process geranyl diphosphate biosynthetic process geranyl diphosphate metabolic process geranylgeranyl diphosphate biosynthetic process geranylgeranyl diphosphate metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR000092	Polyprenyl synthetase	Family
A, B	IPR008949	Isoprenoid synthase domain superfamily	Homologous Superfamily
A, B	IPR033749	Polyprenyl synthetase, conserved site	Conserved Site

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.