4ARX

Lepidoptera-specific toxin Cry1Ac from Bacillus thuringiensis ssp. kurstaki HD-73

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d4arxa3	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	automated matches	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)
A	d4arxa2	All beta proteins	beta-Prism I	delta-Endotoxin (insectocide), middle domain	automated matches	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)
A	d4arxa1	Membrane and cell surface proteins and peptides	Toxins' membrane translocation domains	delta-Endotoxin (insectocide), N-terminal domain	delta-Endotoxin (insectocide), N-terminal domain	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)
B	d4arxb3	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	automated matches	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)
B	d4arxb2	All beta proteins	beta-Prism I	delta-Endotoxin (insectocide), middle domain	automated matches	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)
B	d4arxb1	Membrane and cell surface proteins and peptides	Toxins' membrane translocation domains	delta-Endotoxin (insectocide), N-terminal domain	delta-Endotoxin (insectocide), N-terminal domain	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)
C	d4arxc3	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	automated matches	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)
C	d4arxc2	All beta proteins	beta-Prism I	delta-Endotoxin (insectocide), middle domain	automated matches	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)
C	d4arxc1	Membrane and cell surface proteins and peptides	Toxins' membrane translocation domains	delta-Endotoxin (insectocide), N-terminal domain	delta-Endotoxin (insectocide), N-terminal domain	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)
D	d4arxd3	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	automated matches	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)
D	d4arxd2	All beta proteins	beta-Prism I	delta-Endotoxin (insectocide), middle domain	automated matches	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)
D	d4arxd1	Membrane and cell surface proteins and peptides	Toxins' membrane translocation domains	delta-Endotoxin (insectocide), N-terminal domain	delta-Endotoxin (insectocide), N-terminal domain	automated matches	(Bacillus thuringiensis serovar kurstaki ) [TaxId: 29339 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF03944	e4arxA1	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF03944	ECOD (1.6)
A	PF00555	e4arxA2	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: PF00555	ECOD (1.6)
A	PF03945	e4arxA3	A: alpha arrays	X: Toxins' membrane translocation domains	H: delta-Endotoxin (insectocide), N-terminal domain (From Topology)	T: delta-Endotoxin (insectocide), N-terminal domain	F: PF03945	ECOD (1.6)
B	PF03944	e4arxB1	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF03944	ECOD (1.6)
B	PF00555	e4arxB2	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: PF00555	ECOD (1.6)
B	PF03945	e4arxB3	A: alpha arrays	X: Toxins' membrane translocation domains	H: delta-Endotoxin (insectocide), N-terminal domain (From Topology)	T: delta-Endotoxin (insectocide), N-terminal domain	F: PF03945	ECOD (1.6)
C	PF03944	e4arxC1	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF03944	ECOD (1.6)
C	PF00555	e4arxC2	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: PF00555	ECOD (1.6)
C	PF03945	e4arxC3	A: alpha arrays	X: Toxins' membrane translocation domains	H: delta-Endotoxin (insectocide), N-terminal domain (From Topology)	T: delta-Endotoxin (insectocide), N-terminal domain	F: PF03945	ECOD (1.6)
D	PF03944	e4arxD1	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF03944	ECOD (1.6)
D	PF00555	e4arxD2	A: beta duplicates or obligate multimers	X: beta-Prism I (From Topology)	H: beta-Prism I (From Topology)	T: beta-Prism I	F: PF00555	ECOD (1.6)
D	PF03945	e4arxD3	A: alpha arrays	X: Toxins' membrane translocation domains	H: delta-Endotoxin (insectocide), N-terminal domain (From Topology)	T: delta-Endotoxin (insectocide), N-terminal domain	F: PF03945	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.190.10	Mainly Alpha	Up-down Bundle	Delta-Endotoxin	domain 1	CATH (4.3.0)
A	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
A	2.100.10.10	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Pesticidal crystal protein, central domain	CATH (4.3.0)
B	1.20.190.10	Mainly Alpha	Up-down Bundle	Delta-Endotoxin	domain 1	CATH (4.3.0)
B	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
B	2.100.10.10	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Pesticidal crystal protein, central domain	CATH (4.3.0)
C	1.20.190.10	Mainly Alpha	Up-down Bundle	Delta-Endotoxin	domain 1	CATH (4.3.0)
C	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
C	2.100.10.10	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Pesticidal crystal protein, central domain	CATH (4.3.0)
D	1.20.190.10	Mainly Alpha	Up-down Bundle	Delta-Endotoxin	domain 1	CATH (4.3.0)
D	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
D	2.100.10.10	Mainly Beta	Aligned Prism	Vitelline Membrane Outer Layer Protein I, subunit A	Pesticidal crystal protein, central domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF03944	delta endotoxin (Endotoxin_C)	delta endotoxin	This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N termin ...	This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N terminus is cleaved in all of the proteins and a C terminal extension is cleaved in some members. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain is involved in membrane insertion and pore formation. The second and third domains are involved in receptor binding.	Domain
A, B, C, D	PF03945	delta endotoxin, N-terminal domain (Endotoxin_N)	delta endotoxin, N-terminal domain	This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N termin ...	This family contains insecticidal toxins produced by Bacillus species of bacteria. During spore formation the bacteria produce crystals of this protein. When an insect ingests these proteins they are activated by proteolytic cleavage. The N terminus is cleaved in all of the proteins and a C terminal extension is cleaved in some members. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. This activated region of the delta endotoxin is composed of three structural domains. The N-terminal helical domain is involved in membrane insertion and pore formation. The second and third domains are involved in receptor binding.	Domain
A, B, C, D	PF00555	delta endotoxin (Endotoxin_M)	delta endotoxin	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	PESTICIDAL CRYSTAL PROTEIN CRY1AC	protein binding binding signaling receptor binding toxin activity	sporulation resulting in formation of a cellular spore developmental process anatomical structure morphogenesis anatomical structure formation involved in morphogenesis anatomical structure development sporulation biological process involved in interspecies interaction between organisms cellular process disruption of cell in another organism disruption of anatomical structure in another organism symbiont-mediated killing of host cell killing of cells of another organism cell killing biological process involved in interaction with host sporulation resulting in formation of a cellular spore developmental process anatomical structure morphogenesis anatomical structure formation involved in morphogenesis anatomical structure development sporulation biological process involved in interspecies interaction between organisms cellular process disruption of cell in another organism disruption of anatomical structure in another organism symbiont-mediated killing of host cell killing of cells of another organism cell killing biological process involved in interaction with host biological process involved in symbiotic interaction	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036399	Pesticidal crystal protein, central domain superfamily	Homologous Superfamily
A, B, C, D	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR038979	Pesticidal crystal protein	Family
A, B, C, D	IPR005638	Pesticidal crystal protein, C-terminal	Domain
A, B, C, D	IPR048645	Cry1Ac-like, domain VII	Domain
A, B, C, D	IPR001178	Pesticidal crystal protein, central domain	Domain
A, B, C, D	IPR041587	Pesticidal crystal protein Cry, domain V	Domain
A, B, C, D	IPR005639	Pesticidal crystal protein, N-terminal	Domain
A, B, C, D	IPR036716	Pesticidal crystal protein, N-terminal 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.