2XRS

Crystal structures exploring the origins of the broader specificity of escherichia coli heat-labile enterotoxin compared to cholera toxin

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 [auth E]	d2xrse_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C [auth F]	d2xrsf_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D [auth G]	d2xrsg_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E [auth H]	d2xrsh_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
F [auth L]	d2xrsl_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
G [auth M]	d2xrsm_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
I [auth O]	d2xrso_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
J [auth P]	d2xrsp_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A [auth D]	d2xrsd_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
H [auth N]	d2xrsn_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth E]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	SCOP2B (2022-06-29)
C [auth F]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	SCOP2B (2022-06-29)
D [auth G]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	SCOP2B (2022-06-29)
E [auth H]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	SCOP2B (2022-06-29)
F [auth L]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	SCOP2B (2022-06-29)
G [auth M]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	SCOP2B (2022-06-29)
I [auth O]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	SCOP2B (2022-06-29)
J [auth P]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	SCOP2B (2022-06-29)
A [auth D]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	SCOP2B (2022-06-29)
H [auth N]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	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)
B [auth E]	Enterotoxin_b	e2xrsE1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: Enterotoxin_b	ECOD (1.6)
C [auth F]	Enterotoxin_b	e2xrsF1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: Enterotoxin_b	ECOD (1.6)
D [auth G]	Enterotoxin_b	e2xrsG1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: Enterotoxin_b	ECOD (1.6)
E [auth H]	Enterotoxin_b	e2xrsH1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: Enterotoxin_b	ECOD (1.6)
F [auth L]	Enterotoxin_b	e2xrsL1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: Enterotoxin_b	ECOD (1.6)
G [auth M]	Enterotoxin_b	e2xrsM1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: Enterotoxin_b	ECOD (1.6)
I [auth O]	Enterotoxin_b	e2xrsO1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: Enterotoxin_b	ECOD (1.6)
J [auth P]	Enterotoxin_b	e2xrsP1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: Enterotoxin_b	ECOD (1.6)
A [auth D]	Enterotoxin_b	e2xrsD1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: Enterotoxin_b	ECOD (1.6)
H [auth N]	Enterotoxin_b	e2xrsN1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: Enterotoxin_b	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth E]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
C [auth F]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
D [auth G]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
E [auth H]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
F [auth L]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
G [auth M]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
I [auth O]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
J [auth P]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
A [auth D]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
H [auth N]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth D], B [auth E], C [auth F], D [auth G], E [auth H], A [auth D], B [auth E], C [auth F], D [auth G], E [auth H], F [auth L], G [auth M], H [auth N], I [auth O], J [auth P]	PF01376	Heat-labile enterotoxin beta chain (Enterotoxin_b)	Heat-labile enterotoxin beta chain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth D], B [auth E], C [auth F], D [auth G], E [auth H], A [auth D], B [auth E], C [auth F], D [auth G], E [auth H], F [auth L], G [auth M], H [auth N], I [auth O], J [auth P]	HEAT-LABILE ENTEROTOXIN B CHAIN	toxin activity	biological process involved in interspecies interaction between organisms cellular process disruption of cell in another organism disruption of anatomical structure in another organism killing of cells of another organism cell killing	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth D], B [auth E], C [auth F], D [auth G], E [auth H], A [auth D], B [auth E], C [auth F], D [auth G], E [auth H], F [auth L], G [auth M], H [auth N], I [auth O], J [auth P]	IPR001835	Heat-labile enterotoxin, B chain	Family
A [auth D], B [auth E], C [auth F], D [auth G], E [auth H], A [auth D], B [auth E], C [auth F], D [auth G], E [auth H], F [auth L], G [auth M], H [auth N], I [auth O], J [auth P]	IPR008992	Enterotoxin	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.