1S5E

Cholera holotoxin, Crystal form 1

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)
G [auth B]	d1s5eb_	Alpha and beta proteins (a+b)	ADP-ribosylation	ADP-ribosylation	ADP-ribosylating toxins	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
A	d1s5ea_	Alpha and beta proteins (a+b)	ADP-ribosylation	ADP-ribosylation	ADP-ribosylating toxins	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
B [auth D]	d1s5ed_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
C [auth E]	d1s5ee_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
D [auth F]	d1s5ef_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
F [auth H]	d1s5eh_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
H [auth J]	d1s5ej_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
I [auth K]	d1s5ek_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
J [auth L]	d1s5el_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
K [auth M]	d1s5em_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
L [auth N]	d1s5en_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
E [auth G]	d1s5eg_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Cholera toxin	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
G [auth B]	SCOP2B Superfamily	ADP-ribosylation	8041372	3001208	SCOP2B (2022-06-29)
A	SCOP2 Family	ADP-ribosylating toxins	8028993	4002404	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	ADP-ribosylation	8041372	3001208	SCOP2 (2022-06-29)
B [auth D]	SCOP2B Superfamily	Bacterial enterotoxins	8080121	3000434	SCOP2B (2022-06-29)
C [auth E]	SCOP2B Superfamily	Bacterial enterotoxins	8080121	3000434	SCOP2B (2022-06-29)
D [auth F]	SCOP2B Superfamily	Bacterial enterotoxins	8080121	3000434	SCOP2B (2022-06-29)
F [auth H]	SCOP2B Superfamily	Bacterial enterotoxins	8080121	3000434	SCOP2B (2022-06-29)
H [auth J]	SCOP2B Superfamily	Bacterial enterotoxins	8080121	3000434	SCOP2B (2022-06-29)
I [auth K]	SCOP2B Superfamily	Bacterial enterotoxins	8080121	3000434	SCOP2B (2022-06-29)
J [auth L]	SCOP2B Superfamily	Bacterial enterotoxins	8080121	3000434	SCOP2B (2022-06-29)
K [auth M]	SCOP2B Superfamily	Bacterial enterotoxins	8080121	3000434	SCOP2B (2022-06-29)
L [auth N]	SCOP2B Superfamily	Bacterial enterotoxins	8080121	3000434	SCOP2B (2022-06-29)
E [auth G]	SCOP2B Superfamily	Bacterial enterotoxins	8080121	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)
G [auth B]	PF01375	e1s5eB1	A: a+b complex topology	X: ADP-ribosylation (From Topology)	H: ADP-ribosylation (From Topology)	T: ADP-ribosylation	F: PF01375	ECOD (1.6)
A	PF01375	e1s5eA1	A: a+b complex topology	X: ADP-ribosylation (From Topology)	H: ADP-ribosylation (From Topology)	T: ADP-ribosylation	F: PF01375	ECOD (1.6)
B [auth D]	PF01376	e1s5eD1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
C [auth E]	PF01376	e1s5eE1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
D [auth F]	PF01376	e1s5eF1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
F [auth H]	PF01376	e1s5eH1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
H [auth J]	PF01376	e1s5eJ1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
I [auth K]	PF01376	e1s5eK1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
J [auth L]	PF01376	e1s5eL1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
K [auth M]	PF01376	e1s5eM1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
L [auth N]	PF01376	e1s5eN1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: PF01376	ECOD (1.6)
E [auth G]	PF01376	e1s5eG1	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)
G [auth B]	3.90.210.10	Alpha Beta	Alpha-Beta Complex	Heat-Labile Enterotoxin	Chain A	CATH (4.3.0)
A	3.90.210.10	Alpha Beta	Alpha-Beta Complex	Heat-Labile Enterotoxin	Chain A	CATH (4.3.0)
B [auth D]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
C [auth E]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
D [auth F]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
F [auth H]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
H [auth J]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
I [auth K]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
J [auth L]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
K [auth M]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
L [auth N]	2.40.50.110	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
E [auth G]	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, G [auth B]	PF01375	Heat-labile enterotoxin alpha chain (Enterotoxin_a)	Heat-labile enterotoxin alpha chain	-	Domain
B [auth D], C [auth E], D [auth F], E [auth G], F [auth H], B [auth D], C [auth E], D [auth F], E [auth G], F [auth H], H [auth J], I [auth K], J [auth L], K [auth M], L [auth N]	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, G [auth B]	Cholera enterotoxin, A chain precursor	glycosyltransferase activity transferase activity catalytic activity binding galactose binding monosaccharide binding carbohydrate binding small molecule binding lipid binding nucleotidyltransferase activity transferase activity, transferring phosphorus-containing groups toxin activity	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 localization	periplasmic space cellular anatomical entity protein-containing complex catalytic complex extracellular region extracellular space
B [auth D], C [auth E], D [auth F], E [auth G], F [auth H], B [auth D], C [auth E], D [auth F], E [auth G], F [auth H], H [auth J], I [auth K], J [auth L], K [auth M], L [auth N]	cholera toxin B protein (CTB)	binding galactose binding monosaccharide binding carbohydrate binding small molecule binding host cell surface binding toxin activity	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	membrane cellular anatomical entity host cell plasma membrane host cellular component host cell part host cell membrane periplasmic space protein-containing complex catalytic complex extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, G [auth B]	IPR001144	Heat-labile enterotoxin, A chain	Family
B [auth D], C [auth E], D [auth F], E [auth G], F [auth H], B [auth D], C [auth E], D [auth F], E [auth G], F [auth H], H [auth J], I [auth K], J [auth L], K [auth M], L [auth N]	IPR001835	Heat-labile enterotoxin, B chain	Family
B [auth D], C [auth E], D [auth F], E [auth G], F [auth H], B [auth D], C [auth E], D [auth F], E [auth G], F [auth H], H [auth J], I [auth K], J [auth L], K [auth M], L [auth N]	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.