2Q6M | pdb_00002q6m

Catalytic fragment of Cholix toxin from Vibrio Cholerae in complex with the PJ34 inhibitor

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	d2q6ma1	Alpha and beta proteins (a+b)	ADP-ribosylation	ADP-ribosylation	automated matches	automated matches	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
A	d2q6ma2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(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	Exotox-A_cataly	e2q6mA1	A: a+b complex topology	X: ADP-ribosylation (From Topology)	H: ADP-ribosylation (From Topology)	T: ADP-ribosylation	F: Exotox-A_cataly	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.175.10	Alpha Beta	Alpha-Beta Complex	Diphtheria Toxin	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF09009	Exotoxin A catalytic (Exotox-A_cataly)	Exotoxin A catalytic	Members of this family, which are found in prokaryotic exotoxin A, catalyse the transfer of ADP ribose from nicotinamide adenine dinucleotide (NAD) to elongation factor-2 in eukaryotic cells, with subsequent inhibition of protein synthesis [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Cholix toxin	transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups pentosyltransferase activity glycosyltransferase activity NAD+-diphthamide ADP-ribosyltransferase activity toxin activity	symbiont-mediated perturbation of host cellular process regulation of biological process symbiont-mediated activation of host programmed cell death biological process involved in interspecies interaction between organisms regulation of cellular process symbiont-mediated activation of host apoptosis symbiont-mediated perturbation of host programmed cell death biological regulation regulation of killing of cells of another organism disruption of cell in another organism biological process involved in interaction with host biological process involved in symbiotic interaction symbiont-mediated perturbation of host process cellular process symbiont-mediated perturbation of host cellular process regulation of biological process symbiont-mediated activation of host programmed cell death biological process involved in interspecies interaction between organisms regulation of cellular process symbiont-mediated activation of host apoptosis symbiont-mediated perturbation of host programmed cell death biological regulation regulation of killing of cells of another organism disruption of cell in another organism biological process involved in interaction with host biological process involved in symbiotic interaction symbiont-mediated perturbation of host process cellular process regulation of cell killing symbiont-mediated perturbation of host apoptosis disruption of anatomical structure in another organism modulation of process of another organism symbiont-mediated killing of host cell killing of cells of another organism cell killing	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036478	Exotoxin A, middle domain superfamily	Homologous Superfamily
A	IPR013320	Concanavalin A-like lectin/glucanase domain superfamily	Homologous Superfamily
A	IPR015099	Exotoxin A catalytic domain	Domain
A	IPR015185	Exotoxin A, binding	Domain
A	IPR015186	Exotoxin A, middle domain	Domain

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.