4DZW

Crystal Structure of Trypanosome cruzi farnesyl diphosphate synthase in complex with [2-(cyclohexylamino)ethane-1,1-diyl]bisphosphonic acid and Mg2+

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4dzwa_	All alpha proteins	Terpenoid synthases	Terpenoid synthases	automated matches	automated matches	(Trypanosoma cruzi ) [TaxId: 5693 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Terpenoid synthases	8073834	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	e4dzwA1	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	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	Farnesyl pyrophosphate synthase	dimethylallyltranstransferase activity prenyltransferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity cation binding ion binding binding metal ion binding small molecule binding geranyltranstransferase activity	isoprenoid biosynthetic process lipid biosynthetic process primary metabolic process terpenoid biosynthetic process phospholipid biosynthetic process farnesyl diphosphate metabolic process phospholipid metabolic process biosynthetic process farnesyl diphosphate biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process metabolic process cellular process isoprenoid biosynthetic process lipid biosynthetic process primary metabolic process terpenoid biosynthetic process phospholipid biosynthetic process farnesyl diphosphate metabolic process phospholipid metabolic process biosynthetic process farnesyl diphosphate biosynthetic process organophosphate metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process terpenoid metabolic process lipid metabolic process isoprenoid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR039702	Farnesyl pyrophosphate synthase-like	Family
A	IPR008949	Isoprenoid synthase domain superfamily	Homologous Superfamily
A	IPR033749	Polyprenyl synthetase, conserved site	Conserved Site
A	IPR000092	Polyprenyl synthetase-like	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	FME	Parent Component: MET RESID: AA0021 , AA0566 PSI-MOD : N-formyl-L-methionine residue MOD:00030 , N-formyl-L-methionine (Met) MOD:00482 , N-[(L-histidin-1'-yl)methyl]-L-methionine (fMet) MOD:01890 , N-[(L-histidin-1'-yl)methyl]-L-methionine (Met) MOD:01891

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.