1LTA

2.2 ANGSTROMS CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN (LT) WITH BOUND GALACTOSE

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)
E [auth H]	d1ltah_	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]	d1ltad_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B [auth E]	d1ltae_	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]	d1ltaf_	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]	d1ltag_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Heat-labile toxin	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
F [auth A]	d1lta.1	Alpha and beta proteins (a+b)	ADP-ribosylation	ADP-ribosylation	ADP-ribosylating toxins	Heat-labile toxin, A-chain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
G [auth C]	d1lta.1	Alpha and beta proteins (a+b)	ADP-ribosylation	ADP-ribosylation	ADP-ribosylating toxins	Heat-labile toxin, A-chain	(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)
E [auth H]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	SCOP2B (2022-06-29)
A [auth D]	SCOP2B Superfamily	Bacterial enterotoxins	8041780	3000434	SCOP2B (2022-06-29)
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)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
E [auth H]	Enterotoxin_b	e1ltaH1	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	e1ltaD1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: Enterotoxin_b	ECOD (1.6)
B [auth E]	Enterotoxin_b	e1ltaE1	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	e1ltaF1	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	e1ltaG1	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)
E [auth H]	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)
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)
F [auth A]	3.90.210.10	Alpha Beta	Alpha-Beta Complex	Heat-Labile Enterotoxin	Chain A	CATH (4.3.0)
G [auth C]	1.20.5.240	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		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]	PF01376	Heat-labile enterotoxin beta chain (Enterotoxin_b)	Heat-labile enterotoxin beta chain	-	Domain
F [auth A]	PF01375	Heat-labile enterotoxin alpha chain (Enterotoxin_a)	Heat-labile enterotoxin alpha 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]	HEAT-LABILE ENTEROTOXIN, SUBUNIT B	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
F [auth A]	HEAT-LABILE ENTEROTOXIN, SUBUNIT A	toxin activity	-	extracellular region extracellular space cellular anatomical entity
G [auth C]	HEAT-LABILE ENTEROTOXIN, SUBUNIT A	toxin activity	-	extracellular region extracellular space 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]	IPR001835	Heat-labile enterotoxin, B chain	Family
A [auth D], B [auth E], C [auth F], D [auth G], E [auth H]	IPR008992	Enterotoxin	Homologous Superfamily
F [auth A]	IPR001144	Heat-labile enterotoxin, A chain	Family
G [auth C]	IPR001144	Heat-labile enterotoxin, A chain	Family

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.