Annotations: 3ABZ

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3abza4	All beta proteins	Immunoglobulin-like beta-sandwich	Fibronectin III-like	Fibronectin III-like	Beta-glucosidase C-terminal domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
A	d3abza3	All beta proteins	Anthrax protective antigen N-terminal-like	PA14-like	PA14	Beta-glucosidase PA14 domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
A	d3abza1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	NagZ-like	Beta-glucosidase	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
A	d3abza2	Alpha and beta proteins (a/b)	Flavodoxin-like	Beta-D-glucan exohydrolase, C-terminal domain-like	Beta-D-glucan exohydrolase, C-terminal domain-like	Beta-glucosidase middle domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
B	d3abzb4	All beta proteins	Immunoglobulin-like beta-sandwich	Fibronectin III-like	Fibronectin III-like	Beta-glucosidase C-terminal domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
B	d3abzb3	All beta proteins	Anthrax protective antigen N-terminal-like	PA14-like	PA14	Beta-glucosidase PA14 domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
B	d3abzb1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	NagZ-like	Beta-glucosidase	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
B	d3abzb2	Alpha and beta proteins (a/b)	Flavodoxin-like	Beta-D-glucan exohydrolase, C-terminal domain-like	Beta-D-glucan exohydrolase, C-terminal domain-like	Beta-glucosidase middle domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
C	d3abzc4	All beta proteins	Immunoglobulin-like beta-sandwich	Fibronectin III-like	Fibronectin III-like	Beta-glucosidase C-terminal domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
C	d3abzc3	All beta proteins	Anthrax protective antigen N-terminal-like	PA14-like	PA14	Beta-glucosidase PA14 domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
C	d3abzc1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	NagZ-like	Beta-glucosidase	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
C	d3abzc2	Alpha and beta proteins (a/b)	Flavodoxin-like	Beta-D-glucan exohydrolase, C-terminal domain-like	Beta-D-glucan exohydrolase, C-terminal domain-like	Beta-glucosidase middle domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
D	d3abzd4	All beta proteins	Immunoglobulin-like beta-sandwich	Fibronectin III-like	Fibronectin III-like	Beta-glucosidase C-terminal domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
D	d3abzd3	All beta proteins	Anthrax protective antigen N-terminal-like	PA14-like	PA14	Beta-glucosidase PA14 domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
D	d3abzd1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	NagZ-like	Beta-glucosidase	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	SCOPe (2.08)
D	d3abzd2	Alpha and beta proteins (a/b)	Flavodoxin-like	Beta-D-glucan exohydrolase, C-terminal domain-like	Beta-D-glucan exohydrolase, C-terminal domain-like	Beta-glucosidase middle domain	Yeast (Kluyveromyces marxianus ) [TaxId: 4911 ],	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	PF14310	e3abzA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF14310	ECOD (1.6)
A	PF07691	e3abzA2	A: beta sandwiches	X: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	H: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	T: N-terminal beta-sandwich domain in anthrax protective antigen	F: PF07691	ECOD (1.6)
A	PF00933	e3abzA3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00933	ECOD (1.6)
A	PF01915	e3abzA4	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Beta-D-glucan exohydrolase, C-terminal domain (From Topology)	T: Beta-D-glucan exohydrolase, C-terminal domain	F: PF01915	ECOD (1.6)
B	PF14310	e3abzB1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF14310	ECOD (1.6)
B	PF07691	e3abzB4	A: beta sandwiches	X: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	H: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	T: N-terminal beta-sandwich domain in anthrax protective antigen	F: PF07691	ECOD (1.6)
B	PF00933	e3abzB3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00933	ECOD (1.6)
B	PF01915	e3abzB2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Beta-D-glucan exohydrolase, C-terminal domain (From Topology)	T: Beta-D-glucan exohydrolase, C-terminal domain	F: PF01915	ECOD (1.6)
C	PF14310	e3abzC3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF14310	ECOD (1.6)
C	PF07691	e3abzC1	A: beta sandwiches	X: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	H: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	T: N-terminal beta-sandwich domain in anthrax protective antigen	F: PF07691	ECOD (1.6)
C	PF00933	e3abzC2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00933	ECOD (1.6)
C	PF01915	e3abzC4	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Beta-D-glucan exohydrolase, C-terminal domain (From Topology)	T: Beta-D-glucan exohydrolase, C-terminal domain	F: PF01915	ECOD (1.6)
D	PF14310	e3abzD1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF14310	ECOD (1.6)
D	PF07691	e3abzD5	A: beta sandwiches	X: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	H: N-terminal beta-sandwich domain in anthrax protective antigen (From Topology)	T: N-terminal beta-sandwich domain in anthrax protective antigen	F: PF07691	ECOD (1.6)
D	PF00933	e3abzD2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00933	ECOD (1.6)
D	PF01915	e3abzD4	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Beta-D-glucan exohydrolase, C-terminal domain (From Topology)	T: Beta-D-glucan exohydrolase, C-terminal domain	F: PF01915	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.300	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycoside hydrolase, family 3, N-terminal domain	CATH (4.3.0)
A	3.40.50.1700	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycoside hydrolase family 3 C-terminal domain	CATH (4.3.0)
A	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
A	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
B	3.20.20.300	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycoside hydrolase, family 3, N-terminal domain	CATH (4.3.0)
B	3.40.50.1700	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycoside hydrolase family 3 C-terminal domain	CATH (4.3.0)
B	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
B	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
C	3.20.20.300	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycoside hydrolase, family 3, N-terminal domain	CATH (4.3.0)
C	3.40.50.1700	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycoside hydrolase family 3 C-terminal domain	CATH (4.3.0)
C	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
C	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
D	3.20.20.300	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycoside hydrolase, family 3, N-terminal domain	CATH (4.3.0)
D	3.40.50.1700	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycoside hydrolase family 3 C-terminal domain	CATH (4.3.0)
D	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
D	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF07691	PA14 domain (PA14)	PA14 domain	This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dic ...	This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.	Domain
A, B, C, D	PF00933	Glycosyl hydrolase family 3 N terminal domain (Glyco_hydro_3)	Glycosyl hydrolase family 3 N terminal domain	-	Domain
A, B, C, D	PF01915	Glycosyl hydrolase family 3 C-terminal domain (Glyco_hydro_3_C)	Glycosyl hydrolase family 3 C-terminal domain	This domain is involved in catalysis and may be involved in binding beta-glucan [1]. This domain is found associated with Pfam:PF00933.	Domain
A, B, C, D	PF14310	Fibronectin type III-like domain (Fn3-like)	Fibronectin type III-like domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Beta-glucosidase I	hydrolase activity, acting on glycosyl bonds glucosidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity beta-glucosidase activity catalytic activity scopolin beta-glucosidase activity	carbohydrate metabolic process catabolic process glucan catabolic process beta-glucan metabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process organic substance metabolic process glucan metabolic process beta-glucan catabolic process polysaccharide catabolic process metabolic process cellulose catabolic process carbohydrate metabolic process catabolic process glucan catabolic process beta-glucan metabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process organic substance metabolic process glucan metabolic process beta-glucan catabolic process polysaccharide catabolic process metabolic process cellulose catabolic process macromolecule metabolic process organic substance catabolic process cellulose metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR001764	Glycoside hydrolase, family 3, N-terminal	Domain
A, B, C, D	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A, B, C, D	IPR002772	Glycoside hydrolase family 3 C-terminal domain	Domain
A, B, C, D	IPR036962	Glycoside hydrolase, family 3, N-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR011658	PA14 domain	Domain
A, B, C, D	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A, B, C, D	IPR019800	Glycoside hydrolase, family 3, active site	Active Site
A, B, C, D	IPR037524	PA14/GLEYA domain	Domain
A, B, C, D	IPR026891	Fibronectin type III-like domain	Domain
A, B, C, D	IPR036881	Glycoside hydrolase family 3 C-terminal domain superfamily	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.