1C48 | pdb_00001c48

MUTATED SHIGA-LIKE TOXIN B SUBUNIT (G62T)

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)
A	d1c48a_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Verotoxin-1/shiga-toxin, B-pentamer	(Phage h30 ) [TaxId: 12371 ],	SCOPe (2.08)
B	d1c48b_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Verotoxin-1/shiga-toxin, B-pentamer	(Phage h30 ) [TaxId: 12371 ],	SCOPe (2.08)
C	d1c48c_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Verotoxin-1/shiga-toxin, B-pentamer	(Phage h30 ) [TaxId: 12371 ],	SCOPe (2.08)
D	d1c48d_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Verotoxin-1/shiga-toxin, B-pentamer	(Phage h30 ) [TaxId: 12371 ],	SCOPe (2.08)
E	d1c48e_	All beta proteins	OB-fold	Bacterial enterotoxins	Bacterial AB5 toxins, B-subunits	Verotoxin-1/shiga-toxin, B-pentamer	(Phage h30 ) [TaxId: 12371 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Bacterial enterotoxins	8098912	3000434	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Bacterial enterotoxins	8098912	3000434	SCOP2B (2022-06-29)
C	SCOP2 Family	Bacterial AB5 toxins, B-subunits	8098911	4001827	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Bacterial enterotoxins	8098912	3000434	SCOP2 (2022-06-29)
D	SCOP2B Superfamily	Bacterial enterotoxins	8098912	3000434	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Bacterial enterotoxins	8098912	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)
A	SLT_beta	e1c48A1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: SLT_beta	ECOD (1.6)
B	SLT_beta	e1c48B1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: SLT_beta	ECOD (1.6)
C	SLT_beta	e1c48C1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: SLT_beta	ECOD (1.6)
D	SLT_beta	e1c48D1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: SLT_beta	ECOD (1.6)
E	SLT_beta	e1c48E1	A: beta barrels	X: OB-fold	H: Bacterial enterotoxins (From Topology)	T: Bacterial enterotoxins	F: SLT_beta	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.50.70	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
B	2.40.50.70	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
C	2.40.50.70	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
D	2.40.50.70	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)		CATH (4.3.0)
E	2.40.50.70	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, B, C, D, E	PF02258	Shiga-like toxin beta subunit (SLT_beta)	Shiga-like toxin beta subunit	This family represents the B subunit of shiga-like toxin (SLT or verotoxin) produced by some strains of E.coli associated with hemorrhagic colitis and hemolytic uremic syndrome. SLT's are composed of one enzymatic A subunit and five cell binding B su ...	This family represents the B subunit of shiga-like toxin (SLT or verotoxin) produced by some strains of E.coli associated with hemorrhagic colitis and hemolytic uremic syndrome. SLT's are composed of one enzymatic A subunit and five cell binding B subunits.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E	PROTEIN (SHIGA-LIKE TOXIN I B SUBUNIT)	toxin activity	symbiont-mediated modulation of host virulence biological process involved in interspecies interaction between organisms symbiont-mediated perturbation of host process modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction symbiont-mediated cytolysis of host cell symbiont-mediated hemolysis of host erythrocyte disruption of cell in another organism cytolysis cytolysis in another organism cellular process disruption of anatomical structure in another organism symbiont-mediated killing of host cell symbiont-mediated modulation of host virulence biological process involved in interspecies interaction between organisms symbiont-mediated perturbation of host process modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction symbiont-mediated cytolysis of host cell symbiont-mediated hemolysis of host erythrocyte disruption of cell in another organism cytolysis cytolysis in another organism cellular process disruption of anatomical structure in another organism symbiont-mediated killing of host cell killing of cells of another organism cell killing	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E	IPR008992	Enterotoxin	Homologous Superfamily
A, B, C, D, E	IPR003189	Shiga-like toxin, beta subunit	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.