3PZ2

Crystal structure of RabGGTase(DELTA LRR; DELTA IG) in Complex with BMS3 and lipid substrate GGPP

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d3pz2b_	All alpha proteins	alpha/alpha toroid	Terpenoid cyclases/Protein prenyltransferases	Protein prenyltransferases	Rab geranylgeranyltransferase, beta subunit	rat (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Protein prenylyltransferase	8038637	3001312	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Protein prenylyltransferase	8038637	3001312	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Terpenoid cyclases/Protein prenyltransferases	8040875	3001024	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	PPTA	e3pz2A1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PPTA	ECOD (1.6)
B	SQHop_cyclase_C	e3pz2B1	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: SQHop_cyclase_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.25.40.120	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Protein prenylyltransferase	CATH (4.3.0)
B	1.50.10.20	Mainly Alpha	Alpha/alpha barrel	Glycosyltransferase		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01239	Protein prenyltransferase alpha subunit repeat (PPTA)	Protein prenyltransferase alpha subunit repeat	-	Repeat
B	PF00432	Prenyltransferase and squalene oxidase repeat (Prenyltrans)	Prenyltransferase and squalene oxidase repeat	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Geranylgeranyl transferase type-2 subunit alpha	small GTPase binding protein binding binding enzyme binding GTPase binding catalytic activity, acting on a protein protein geranylgeranyltransferase activity protein prenyltransferase activity Rab geranylgeranyltransferase activity prenyltransferase activity transferase activity catalytic activity transferase activity, transferring alkyl or aryl (other than methyl) groups cation binding small GTPase binding protein binding binding enzyme binding GTPase binding catalytic activity, acting on a protein protein geranylgeranyltransferase activity protein prenyltransferase activity Rab geranylgeranyltransferase activity prenyltransferase activity transferase activity catalytic activity transferase activity, transferring alkyl or aryl (other than methyl) groups cation binding transition metal ion binding zinc ion binding ion binding metal ion binding small molecule binding	macromolecule modification protein prenylation protein geranylgeranylation metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process prenylation protein modification process	protein-containing complex cellular anatomical structure intracellular anatomical structure catalytic complex polyprenyl diphosphate synthase complex Rab-protein geranylgeranyltransferase complex cytoplasm transferase complex
B	Geranylgeranyl transferase type-2 subunit beta	small GTPase binding protein binding binding enzyme binding GTPase binding isoprenoid binding lipid binding catalytic activity, acting on a protein protein geranylgeranyltransferase activity protein prenyltransferase activity Rab geranylgeranyltransferase activity prenyltransferase activity transferase activity catalytic activity small GTPase binding protein binding binding enzyme binding GTPase binding isoprenoid binding lipid binding catalytic activity, acting on a protein protein geranylgeranyltransferase activity protein prenyltransferase activity Rab geranylgeranyltransferase activity prenyltransferase activity transferase activity catalytic activity transferase activity, transferring alkyl or aryl (other than methyl) groups cation binding transition metal ion binding zinc ion binding ion binding metal ion binding small molecule binding	macromolecule modification protein prenylation protein geranylgeranylation metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process prenylation protein modification process	protein-containing complex cellular anatomical structure intracellular anatomical structure catalytic complex polyprenyl diphosphate synthase complex Rab-protein geranylgeranyltransferase complex cytoplasm transferase complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR009087	Rab geranylgeranyltransferase, alpha subunit, insert-domain	Domain
A	IPR002088	Protein prenyltransferase, alpha subunit	Repeat
A	IPR032675	Leucine-rich repeat domain superfamily	Homologous Superfamily
A	IPR036254	Rab geranylgeranyltransferase, alpha subunit, insert-domain superfamily	Homologous Superfamily
B	IPR045089	Prenyltransferase subunit beta	Family
B	IPR026873	Geranylgeranyl transferase type-2 subunit beta	Family
B	IPR001330	PFTB repeat	Repeat
B	IPR008930	Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid	Homologous Superfamily

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.