3EFX

Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin, 1.9A crystal structure reveals the details

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 [auth D]	d3efxd1	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
B [auth E]	d3efxe_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	automated matches	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
C [auth F]	d3efxf_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	automated matches	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
D [auth G]	d3efxg_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	automated matches	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
E [auth H]	d3efxh_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	automated matches	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
F [auth I]	d3efxi_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	automated matches	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
G [auth J]	d3efxj_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	automated matches	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
H [auth K]	d3efxk_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	automated matches	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
I [auth L]	d3efxl_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	automated matches	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
J [auth M]	d3efxm_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	automated matches	(Vibrio cholerae ) [TaxId: 666 ],	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 [auth D]	PF01376	e3efxD1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
B [auth E]	PF01376	e3efxE1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
C [auth F]	PF01376	e3efxF1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
D [auth G]	PF01376	e3efxG1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
E [auth H]	PF01376	e3efxH1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
F [auth I]	PF01376	e3efxI1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
G [auth J]	PF01376	e3efxJ1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
H [auth K]	PF01376	e3efxK1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
I [auth L]	PF01376	e3efxL1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
J [auth M]	PF01376	e3efxM1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
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)
E [auth H]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
F [auth I]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
G [auth J]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
H [auth K]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
I [auth L]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
J [auth M]	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 I], G [auth J], H [auth K], I [auth L], J [auth M]	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 I], G [auth J], H [auth K], I [auth L], J [auth M]	Cholera enterotoxin subunit B, Heat-labile enterotoxin B chain	toxin activity binding galactose binding monosaccharide binding carbohydrate binding small molecule binding host cell surface binding	cellular response to stimulus regulation of cellular process response to stimulus positive regulation of phosphorylation positive regulation of phosphate metabolic process cell communication regulation of primary metabolic process positive regulation of metabolic process regulation of phosphate metabolic process peptidyl-amino acid modification phosphate-containing compound metabolic process positive regulation of macromolecule metabolic process signal transduction protein modification process cellular response to stimulus regulation of cellular process response to stimulus positive regulation of phosphorylation positive regulation of phosphate metabolic process cell communication regulation of primary metabolic process positive regulation of metabolic process regulation of phosphate metabolic process peptidyl-amino acid modification phosphate-containing compound metabolic process positive regulation of macromolecule metabolic process signal transduction protein modification process phosphorus metabolic process positive regulation of protein phosphorylation tyrosine phosphorylation of STAT protein regulation of biological process protein phosphorylation positive regulation of phosphorus metabolic process phosphorylation cellular metabolic process regulation of protein metabolic process primary metabolic process regulation of cellular metabolic process macromolecule modification metabolic process regulation of phosphorus metabolic process macromolecule metabolic process regulation of metabolic process cell surface receptor signaling pathway via STAT regulation of protein modification process signaling regulation of protein phosphorylation positive regulation of protein metabolic process positive regulation of biological process positive regulation of cellular metabolic process peptidyl-tyrosine modification positive regulation of peptidyl-tyrosine phosphorylation positive regulation of protein modification process organic substance metabolic process protein metabolic process positive regulation of cellular process organonitrogen compound metabolic process cell surface receptor signaling pathway regulation of tyrosine phosphorylation of STAT protein biological regulation regulation of peptidyl-tyrosine phosphorylation regulation of macromolecule metabolic process positive regulation of tyrosine phosphorylation of STAT protein cellular process regulation of phosphorylation peptidyl-tyrosine phosphorylation cell surface receptor signaling pathway via JAK-STAT	extracellular region cellular anatomical entity membrane host cell plasma membrane host cellular component host cell part host cell membrane periplasmic space protein-containing complex catalytic complex

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 I], G [auth J], H [auth K], I [auth L], J [auth M]	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 I], G [auth J], H [auth K], I [auth L], J [auth M]	IPR008992	Enterotoxin	Homologous Superfamily
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 I], G [auth J], H [auth K], I [auth L], J [auth M]	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 I], G [auth J], H [auth K], I [auth L], J [auth M]	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 R01GM133198.