Annotations: 6F47

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6f47a1	Alpha and beta proteins (a+b)	Zincin-like	Metalloproteases ('zincins'), catalytic domain	automated matches	automated matches	(Clostridium botulinum ) [TaxId: 1491 ],	SCOPe (2.08)
A	d6f47a2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Clostridium botulinum ) [TaxId: 1491 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Clostridium neurotoxins catalytic domain	8107531	4001621	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Metalloproteases (zincins) catalytic domain	8107532	3001975	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	PF01742	e6f47A1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01742	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01742	Clostridial neurotoxin zinc protease (Peptidase_M27)	Clostridial neurotoxin zinc protease	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Catalytic domain of botulinum neurotoxin X	macromolecule transmembrane transporter activity protein transporter activity protein transmembrane transporter activity transporter activity transmembrane transporter activity peptidase activity catalytic activity, acting on a protein metalloendopeptidase activity hydrolase activity metallopeptidase activity catalytic activity endopeptidase activity toxin activity cation binding macromolecule transmembrane transporter activity protein transporter activity protein transmembrane transporter activity transporter activity transmembrane transporter activity peptidase activity catalytic activity, acting on a protein metalloendopeptidase activity hydrolase activity metallopeptidase activity catalytic activity endopeptidase activity toxin activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	membrane cellular anatomical entity extracellular region host cell plasma membrane host cellular component host cell part host cell membrane host cell synapse host cell presynaptic membrane host intracellular part host cell cytoplasm host intracellular region host cell cytosol host cell cytoplasm part membrane cellular anatomical entity extracellular region host cell plasma membrane host cellular component host cell part host cell membrane host cell synapse host cell presynaptic membrane host intracellular part host cell cytoplasm host intracellular region host cell cytosol host cell cytoplasm part host cell cytoplasmic vesicle host intracellular membrane-bounded organelle host intracellular organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000395	Botulinum/Tetanus toxin, catalytic chain	Domain
A	IPR012928	Clostridium neurotoxin, receptor binding N-terminal	Domain
A	IPR012500	Clostridium neurotoxin, translocation	Domain
A	IPR011065	Kunitz inhibitor STI-like superfamily	Homologous Superfamily
A	IPR013104	Clostridium neurotoxin, receptor-binding C-terminal	Domain
A	IPR013320	Concanavalin A-like lectin/glucanase domain superfamily	Homologous Superfamily
A	IPR036248	Clostridium neurotoxin, translocation domain	Homologous Superfamily

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 R01GM133198.