Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
C [auth B]d1r4qb_ All beta proteins OB-fold Bacterial enterotoxins Bacterial AB5 toxins, B-subunits Verotoxin-1/shiga-toxin, B-pentamer (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)
D [auth C]d1r4qc_ All beta proteins OB-fold Bacterial enterotoxins Bacterial AB5 toxins, B-subunits Verotoxin-1/shiga-toxin, B-pentamer (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)
E [auth D]d1r4qd_ All beta proteins OB-fold Bacterial enterotoxins Bacterial AB5 toxins, B-subunits Verotoxin-1/shiga-toxin, B-pentamer (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)
F [auth E]d1r4qe_ All beta proteins OB-fold Bacterial enterotoxins Bacterial AB5 toxins, B-subunits Verotoxin-1/shiga-toxin, B-pentamer (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)
G [auth F]d1r4qf_ All beta proteins OB-fold Bacterial enterotoxins Bacterial AB5 toxins, B-subunits Verotoxin-1/shiga-toxin, B-pentamer (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)
H [auth G]d1r4qg_ All beta proteins OB-fold Bacterial enterotoxins Bacterial AB5 toxins, B-subunits Verotoxin-1/shiga-toxin, B-pentamer (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)
I [auth H]d1r4qh_ All beta proteins OB-fold Bacterial enterotoxins Bacterial AB5 toxins, B-subunits Verotoxin-1/shiga-toxin, B-pentamer (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)
J [auth I]d1r4qi_ All beta proteins OB-fold Bacterial enterotoxins Bacterial AB5 toxins, B-subunits Verotoxin-1/shiga-toxin, B-pentamer (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)
K [auth J]d1r4qj_ All beta proteins OB-fold Bacterial enterotoxins Bacterial AB5 toxins, B-subunits Verotoxin-1/shiga-toxin, B-pentamer (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)
L [auth K]d1r4qk_ All beta proteins OB-fold Bacterial enterotoxins Bacterial AB5 toxins, B-subunits Verotoxin-1/shiga-toxin, B-pentamer (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)
Ad1r4qa_ Alpha and beta proteins (a+b) Ribosome inactivating proteins (RIP) Ribosome inactivating proteins (RIP) Shiga toxin, A-chain Shiga toxin, A-chain (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)
B [auth L]d1r4ql_ Alpha and beta proteins (a+b) Ribosome inactivating proteins (RIP) Ribosome inactivating proteins (RIP) Shiga toxin, A-chain Shiga toxin, A-chain (Shigella dysenteriae ) [TaxId: 622 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
C [auth B]SCOP2B SuperfamilyBacterial enterotoxins 8099966 3000434 SCOP2B (2022-06-29)
D [auth C]SCOP2B SuperfamilyBacterial enterotoxins 8099966 3000434 SCOP2B (2022-06-29)
E [auth D]SCOP2B SuperfamilyBacterial enterotoxins 8099966 3000434 SCOP2B (2022-06-29)
F [auth E]SCOP2B SuperfamilyBacterial enterotoxins 8099966 3000434 SCOP2B (2022-06-29)
G [auth F]SCOP2B SuperfamilyBacterial enterotoxins 8099966 3000434 SCOP2B (2022-06-29)
H [auth G]SCOP2B SuperfamilyBacterial enterotoxins 8099966 3000434 SCOP2B (2022-06-29)
I [auth H]SCOP2B SuperfamilyBacterial enterotoxins 8099966 3000434 SCOP2B (2022-06-29)
J [auth I]SCOP2B SuperfamilyBacterial enterotoxins 8099966 3000434 SCOP2B (2022-06-29)
K [auth J]SCOP2B SuperfamilyBacterial enterotoxins 8099966 3000434 SCOP2B (2022-06-29)
L [auth K]SCOP2B SuperfamilyBacterial enterotoxins 8099966 3000434 SCOP2B (2022-06-29)
ASCOP2 FamilyShiga toxin, A-chain 8027917 4002413 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyRibosome inactivating proteins (RIP) 8040296 3001164 SCOP2 (2022-06-29)
B [auth L]SCOP2B SuperfamilyRibosome inactivating proteins (RIP) 8040296 3001164 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
C [auth B]SLT_betae1r4qB1 A: beta barrelsX: OB-foldH: Bacterial enterotoxins (From Topology)T: Bacterial enterotoxinsF: SLT_betaECOD (1.6)
D [auth C]SLT_betae1r4qC1 A: beta barrelsX: OB-foldH: Bacterial enterotoxins (From Topology)T: Bacterial enterotoxinsF: SLT_betaECOD (1.6)
E [auth D]SLT_betae1r4qD1 A: beta barrelsX: OB-foldH: Bacterial enterotoxins (From Topology)T: Bacterial enterotoxinsF: SLT_betaECOD (1.6)
F [auth E]SLT_betae1r4qE1 A: beta barrelsX: OB-foldH: Bacterial enterotoxins (From Topology)T: Bacterial enterotoxinsF: SLT_betaECOD (1.6)
G [auth F]SLT_betae1r4qF1 A: beta barrelsX: OB-foldH: Bacterial enterotoxins (From Topology)T: Bacterial enterotoxinsF: SLT_betaECOD (1.6)
H [auth G]SLT_betae1r4qG1 A: beta barrelsX: OB-foldH: Bacterial enterotoxins (From Topology)T: Bacterial enterotoxinsF: SLT_betaECOD (1.6)
I [auth H]SLT_betae1r4qH1 A: beta barrelsX: OB-foldH: Bacterial enterotoxins (From Topology)T: Bacterial enterotoxinsF: SLT_betaECOD (1.6)
J [auth I]SLT_betae1r4qI1 A: beta barrelsX: OB-foldH: Bacterial enterotoxins (From Topology)T: Bacterial enterotoxinsF: SLT_betaECOD (1.6)
K [auth J]SLT_betae1r4qJ1 A: beta barrelsX: OB-foldH: Bacterial enterotoxins (From Topology)T: Bacterial enterotoxinsF: SLT_betaECOD (1.6)
L [auth K]SLT_betae1r4qK1 A: beta barrelsX: OB-foldH: Bacterial enterotoxins (From Topology)T: Bacterial enterotoxinsF: SLT_betaECOD (1.6)
ARIPe1r4qA1 A: a+b two layersX: RIP/Polo-box domainH: Ribosome inactivating proteins (RIP) (From Topology)T: Ribosome inactivating proteins (RIP)F: RIPECOD (1.6)
B [auth L]RIPe1r4qL1 A: a+b two layersX: RIP/Polo-box domainH: Ribosome inactivating proteins (RIP) (From Topology)T: Ribosome inactivating proteins (RIP)F: RIPECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
C [auth B]2.40.50.70 Mainly Beta Beta Barrel OB fold (Dihydrolipoamide Acetyltransferase, E2P) CATH (4.3.0)
D [auth C]2.40.50.70 Mainly Beta Beta Barrel OB fold (Dihydrolipoamide Acetyltransferase, E2P) CATH (4.3.0)
E [auth D]2.40.50.70 Mainly Beta Beta Barrel OB fold (Dihydrolipoamide Acetyltransferase, E2P) CATH (4.3.0)
F [auth E]2.40.50.70 Mainly Beta Beta Barrel OB fold (Dihydrolipoamide Acetyltransferase, E2P) CATH (4.3.0)
G [auth F]2.40.50.70 Mainly Beta Beta Barrel OB fold (Dihydrolipoamide Acetyltransferase, E2P) CATH (4.3.0)
H [auth G]2.40.50.70 Mainly Beta Beta Barrel OB fold (Dihydrolipoamide Acetyltransferase, E2P) CATH (4.3.0)
I [auth H]2.40.50.70 Mainly Beta Beta Barrel OB fold (Dihydrolipoamide Acetyltransferase, E2P) CATH (4.3.0)
J [auth I]2.40.50.70 Mainly Beta Beta Barrel OB fold (Dihydrolipoamide Acetyltransferase, E2P) CATH (4.3.0)
K [auth J]2.40.50.70 Mainly Beta Beta Barrel OB fold (Dihydrolipoamide Acetyltransferase, E2P) CATH (4.3.0)
L [auth K]2.40.50.70 Mainly Beta Beta Barrel OB fold (Dihydrolipoamide Acetyltransferase, E2P) CATH (4.3.0)
A3.40.420.10 Alpha Beta 3-Layer(aba) Sandwich Ricin (A subunit) domain 1CATH (4.3.0)
A4.10.470.10 Few Secondary Structures Irregular Ricin (A Subunit), domain 2 Ricin (A Subunit), domain 2CATH (4.3.0)
B [auth L]3.40.420.10 Alpha Beta 3-Layer(aba) Sandwich Ricin (A subunit) domain 1CATH (4.3.0)
B [auth L]4.10.470.10 Few Secondary Structures Irregular Ricin (A Subunit), domain 2 Ricin (A Subunit), domain 2CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF02258Shiga-like toxin beta subunit (SLT_beta)Shiga-like toxin beta subunitThis 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 s ...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
A,
B [auth L]
PF00161Ribosome inactivating protein (RIP)Ribosome inactivating protein- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Shigella toxin chain B
A,
B [auth L]
SHT cytotoxin A subunit -