4FXQ

Full-length Certhrax toxin from Bacillus cereus in complex with Inhibitor P6

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	ADP-ribosylation	8088442	3001208	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	ADP-ribosylation	8088442	3001208	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	PF03496	e4fxqA1	A: a+b complex topology	X: ADP-ribosylation (From Topology)	H: ADP-ribosylation (From Topology)	T: ADP-ribosylation	F: PF03496	ECOD (1.6)
A	PF07737	e4fxqA2	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF07737	ECOD (1.6)
B	PF03496	e4fxqB1	A: a+b complex topology	X: ADP-ribosylation (From Topology)	H: ADP-ribosylation (From Topology)	T: ADP-ribosylation	F: PF03496	ECOD (1.6)
B	PF07737	e4fxqB2	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF07737	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
A	3.90.176.10	Alpha Beta	Alpha-Beta Complex	Toxin ADP-ribosyltransferase	Chain A, domain 1	CATH (4.3.0)
B	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
B	3.90.176.10	Alpha Beta	Alpha-Beta Complex	Toxin ADP-ribosyltransferase	Chain A, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03496	ADP-ribosyltransferase exoenzyme (ADPrib_exo_Tox)	ADP-ribosyltransferase exoenzyme	-	Family
A, B	PF07737	Anthrax toxin lethal factor, N- and C-terminal domain (ATLF)	Anthrax toxin lethal factor, N- and C-terminal domain	The C-terminal domain is the catalytically active domain whereas the N-terminal domain is likely to be inactive.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Putative ADP-ribosyltransferase Certhrax	glycosyltransferase activity transferase activity catalytic activity peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity nucleotidyltransferase activity transferase activity, transferring phosphorus-containing groups binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding glycosyltransferase activity transferase activity catalytic activity peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity nucleotidyltransferase activity transferase activity, transferring phosphorus-containing groups binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding cation binding ion binding metal ion binding toxin activity	-	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR003540	ADP ribosyltransferase	Domain
A, B	IPR024079	Metallopeptidase, catalytic domain superfamily	Homologous Superfamily
A, B	IPR047568	Anthrax toxin lethal factor-like domain	Domain
A, B	IPR003541	Anthrax toxin, lethal/endema factor	Family
A, B	IPR014781	Anthrax toxin, lethal/endema factor, N-/C-terminal	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.