6OQ6 | pdb_00006oq6

Structure of the pore forming fragment of Clostridium difficile toxin B in complex with VHH 5D

External Resource: Annotation

Domain Annotation: ECOD Classification
SAbDab Antibody Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B [auth D]	V-set_12	e6oq6D1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: V-set_12	ECOD (1.6)

SAbDab Antibody Annotation SAbDab Database Homepage

Chain	Chain Class	Chain Subclass	Chain Type	Antigen Name(s)	Provenance Source
B [auth D]	Heavy Chain	IGHV1	-	toxin b	SAbDab (2025-10-17)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B [auth D]	5D	-	-	-
A	Toxin B	binding lipid binding toxin activity glycosyltransferase activity transferase activity glucosyltransferase activity hexosyltransferase activity catalytic activity cysteine-type peptidase activity peptidase activity catalytic activity, acting on a protein hydrolase activity cation binding ion binding binding lipid binding toxin activity glycosyltransferase activity transferase activity glucosyltransferase activity hexosyltransferase activity catalytic activity cysteine-type peptidase activity peptidase activity catalytic activity, acting on a protein hydrolase activity cation binding ion binding metal ion binding small molecule binding	symbiont-mediated perturbation of host actin cytoskeleton symbiont-mediated disruption of host anatomical structure biological process involved in interspecies interaction between organisms symbiont-mediated perturbation of host actin cytoskeleton via filamentous actin depolymerization symbiont-mediated perturbation of host cytoskeleton disruption of anatomical structure in another organism symbiont-mediated disruption of host cellular anatomical structure proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process	cellular anatomical structure membrane extracellular region host intracellular membrane-bounded organelle host cellular component host intracellular part host cell membrane other organism part host cell cytoplasm part host intracellular organelle host cell endosome membrane host cell cytoplasm host cell part host cell endosome cellular anatomical structure membrane extracellular region host intracellular membrane-bounded organelle host cellular component host intracellular part host cell membrane other organism part host cell cytoplasm part host intracellular organelle host cell endosome membrane host cell cytoplasm host cell part host cell endosome host intracellular region host cell plasma membrane host cell cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR038383	CGT/MARTX, cysteine protease (CPD) domain superfamily	Homologous Superfamily
A	IPR024772	TcdA/TcdB toxin, N-terminal helical domain	Domain
A	IPR020974	CGT/MARTX, cysteine protease (CPD) domain	Domain
A	IPR024769	TcdA/TcdB toxin, pore forming domain	Domain
A	IPR029044	Nucleotide-diphospho-sugar transferases	Homologous Superfamily
A	IPR024770	TcdA/TcdB toxin, catalytic glycosyltransferase domain	Domain
A	IPR018337	Cell wall/choline-binding repeat	Repeat

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A	OPM	Monotopic/peripheral	Alpha/Beta monotopic/peripheral	Nucleotide-diphospho-sugar transferases	Glycosylating toxin

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.