5IMP

Crystal structure of N299A Aspergillus terreus aristolochene synthase complexed with (1S,8S,9aR)-1,9a-dimethyl-8-(prop-1-en-2-yl)decahydroquinolizin-5-ium

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)
A	d5impa_	All alpha proteins	Terpenoid synthases	Terpenoid synthases	Aristolochene/pentalenene synthase	automated matches	(Aspergillus terreus ) [TaxId: 33178 ],	SCOPe (2.08)
B	d5impb_	All alpha proteins	Terpenoid synthases	Terpenoid synthases	Aristolochene/pentalenene synthase	automated matches	(Aspergillus terreus ) [TaxId: 33178 ],	SCOPe (2.08)
C	d5impc_	All alpha proteins	Terpenoid synthases	Terpenoid synthases	Aristolochene/pentalenene synthase	automated matches	(Aspergillus terreus ) [TaxId: 33178 ],	SCOPe (2.08)
D	d5impd_	All alpha proteins	Terpenoid synthases	Terpenoid synthases	Aristolochene/pentalenene synthase	automated matches	(Aspergillus terreus ) [TaxId: 33178 ],	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	8084311	3001615	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Terpenoid synthases	8084311	3001615	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Terpenoid synthases	8084311	3001615	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Terpenoid synthases	8084311	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	PF19086	e5impA1	A: alpha bundles	X: Terpenoid synthases (From Topology)	H: Terpenoid synthases (From Topology)	T: Terpenoid synthases	F: PF19086	ECOD (1.6)
B	PF19086	e5impB1	A: alpha bundles	X: Terpenoid synthases (From Topology)	H: Terpenoid synthases (From Topology)	T: Terpenoid synthases	F: PF19086	ECOD (1.6)
C	PF19086	e5impC1	A: alpha bundles	X: Terpenoid synthases (From Topology)	H: Terpenoid synthases (From Topology)	T: Terpenoid synthases	F: PF19086	ECOD (1.6)
D	PF19086	e5impD1	A: alpha bundles	X: Terpenoid synthases (From Topology)	H: Terpenoid synthases (From Topology)	T: Terpenoid synthases	F: PF19086	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)
C	1.10.600.10	Mainly Alpha	Orthogonal Bundle	Farnesyl Diphosphate Synthase	Farnesyl Diphosphate Synthase	CATH (4.3.0)
D	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, C, D	PF19086	Terpene synthase family 2, C-terminal metal binding (Terpene_syn_C_2)	Terpene synthase family 2, C-terminal metal binding	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Aristolochene synthase	carbon-oxygen lyase activity, acting on phosphates sesquiterpene synthase activity terpene synthase activity lyase activity catalytic activity carbon-oxygen lyase activity aristolochene synthase activity cation binding ion binding binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR008949	Isoprenoid synthase domain superfamily	Homologous Superfamily

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.