1K8T

Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF)

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	d1k8ta_	Multi-domain proteins (alpha and beta)	Adenylylcyclase toxin (the edema factor)	Adenylylcyclase toxin (the edema factor)	Adenylylcyclase toxin (the edema factor)	Adenylylcyclase toxin (the edema factor)	(Bacillus anthracis ) [TaxId: 1392 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Adenylylcyclase toxin N-terminal domain-like	8025532	4003589	SCOP2 (2022-06-29)
A	SCOP2 Family	Adenylylcyclase toxin C-terminal domain-like	8054299	4007636	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Nucleotidyltransferase-like	8037911	3000129	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PAP/OAS1 substrate-binding domain-like	8054301	3000941	SCOP2 (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	EUF08089	e1k8tA1	A: alpha bundles	X: Alpha-helical domain in adenylylcyclase toxin (From Topology)	H: Alpha-helical domain in adenylylcyclase toxin (From Topology)	T: Alpha-helical domain in adenylylcyclase toxin	F: EUF08089	ECOD (1.6)
A	Anthrax_toxA_C	e1k8tA2	A: a+b two layers	X: Insertion domain in adenylylcyclase toxin (the edema factor) (From Topology)	H: Insertion domain in adenylylcyclase toxin (the edema factor) (From Topology)	T: Insertion domain in adenylylcyclase toxin (the edema factor)	F: Anthrax_toxA_C	ECOD (1.6)
A	Anthrax_toxA_N	e1k8tA3	A: a+b three layers	X: N-terminal a+b domain in adenylylcyclase toxin (From Topology)	H: N-terminal a+b domain in adenylylcyclase toxin (From Topology)	T: N-terminal a+b domain in adenylylcyclase toxin	F: Anthrax_toxA_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1760.10	Alpha Beta	Alpha-Beta Complex	Adenylylcyclase toxin fold	Anthrax toxin, edema factor, central domain	CATH (4.3.0)
A	1.20.140.60	Mainly Alpha	Up-down Bundle	Butyryl-CoA Dehydrogenase, subunit A	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF20850	Oedema factor (EF), alpha-helical domain (EF_HD)	Oedema factor (EF), alpha-helical domain	This domain is found in Oedema factor (EF), the exotoxin with adenylyl cyclase activity produced by Bacillus anthracis to increase the concentration of cyclic AMP in infected host cells and disrupts intracellular signalling pathways. EF consists of f ...	This domain is found in Oedema factor (EF), the exotoxin with adenylyl cyclase activity produced by Bacillus anthracis to increase the concentration of cyclic AMP in infected host cells and disrupts intracellular signalling pathways. EF consists of four domains: a PA-binding domain (PABD), two adenylate cyclase domains (ACD) and a helical domain (HD, this entry). HD moves and forms a large clamp that almost completely encircles EF's activator calmodulin (CaM), naturally present in host cells, stabilizing a disordered loop and leading to enzyme activation [1,4].	Domain
A	PF03497	Anthrax toxin LF subunit (Anthrax_toxA)	Anthrax toxin LF subunit	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	CALMODULIN-SENSITIVE ADENYLATE CYCLASE	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity phosphorus-oxygen lyase activity cyclase activity lyase activity adenylate cyclase activity calcium- and calmodulin-responsive adenylate cyclase activity toxin activity protein binding calmodulin binding cation binding metal ion binding	ribose phosphate metabolic process nucleotide biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process cAMP biosynthetic process cyclic nucleotide metabolic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleotide metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process cyclic nucleotide biosynthetic process phosphate-containing compound metabolic process ribose phosphate metabolic process nucleotide biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process cAMP biosynthetic process cyclic nucleotide metabolic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleotide metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process cyclic nucleotide biosynthetic process phosphate-containing compound metabolic process small molecule metabolic process phosphorus metabolic process ribose phosphate biosynthetic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process cAMP metabolic process cyclic purine nucleotide metabolic process cellular metabolic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process purine ribonucleotide metabolic process purine nucleotide biosynthetic process	extracellular region cellular anatomical entity protein-containing complex catalytic complex host cellular component host intracellular part host cell cytoplasm host cell part host intracellular region host cell cytosol host cell cytoplasm part

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR005165	Anthrax toxin, edema factor, central	Domain
A	IPR024079	Metallopeptidase, catalytic domain superfamily	Homologous Superfamily
A	IPR035099	Anthrax toxin, edema factor, C-terminal	Homologous Superfamily
A	IPR003541	Anthrax toxin, lethal/endema factor	Family
A	IPR014781	Anthrax toxin, lethal/endema factor, N-/C-terminal	Domain
A	IPR037017	Anthrax toxin, edema factor, central domain superfamily	Homologous Superfamily
A	IPR047568	Anthrax toxin lethal factor-like domain	Domain
A	IPR049405	Edema factor, alpha-helical 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.