Annotations: 4ON1

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	fragilysinNterm_1	e4on1A2	A: a+b two layers	X: Fragilysin-3 prodomain-like	H: Fragilysin-3 prodomain (From Topology)	T: Fragilysin-3 prodomain	F: fragilysinNterm_1	ECOD (1.6)
A	Reprolysin	e4on1A1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Reprolysin	ECOD (1.6)
B	fragilysinNterm_1	e4on1B2	A: a+b two layers	X: Fragilysin-3 prodomain-like	H: Fragilysin-3 prodomain (From Topology)	T: Fragilysin-3 prodomain	F: fragilysinNterm_1	ECOD (1.6)
B	Reprolysin	e4on1B1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Reprolysin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.128.470	Mainly Beta	Beta Barrel	Lipocalin		CATH (4.3.0)
A	3.40.390.10	Alpha Beta	3-Layer(aba) Sandwich	Collagenase (Catalytic Domain)	Collagenase (Catalytic Domain)	CATH (4.3.0)
B	2.40.128.470	Mainly Beta	Beta Barrel	Lipocalin		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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00413	Matrixin (Peptidase_M10)	Matrixin	The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.	Domain
A, B	PF16376	N-terminal domain of fragilysin (fragilysinNterm)	N-terminal domain of fragilysin	N-terminal domain of fragilysin, an extracellular metalloprotease toxin, which is primary virulence factor of B. fragilis, an oportunistic pathogen of human gut. The N-terminal domain of fragilysin inhibits fragilysin and is cleaved ...	N-terminal domain of fragilysin, an extracellular metalloprotease toxin, which is primary virulence factor of B. fragilis, an oportunistic pathogen of human gut. The N-terminal domain of fragilysin inhibits fragilysin and is cleaved in a mature, virulent form.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Putative metalloprotease II	cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein metalloendopeptidase activity hydrolase activity metallopeptidase activity catalytic activity endopeptidase activity	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	cell periphery extracellular matrix external encapsulating structure cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR038176	Fragilysin, N-terminal domain superfamily	Homologous Superfamily
A, B	IPR006026	Peptidase, metallopeptidase	Domain
A, B	IPR024079	Metallopeptidase, catalytic domain superfamily	Homologous Superfamily
A, B	IPR032273	Fragilysin, N-terminal	Domain
A, B	IPR001818	Peptidase M10, metallopeptidase	Domain
A, B	IPR001843	Fragilysin	Family

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.