Annotations: 3GM8

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	E-set domains of sugar-utilizing enzymes	8045422	4007565	SCOP2 (2022-06-29)
A	SCOP2 Family	E-set domains of sugar-utilizing enzymes	8090584	4007565	SCOP2 (2022-06-29)
A	SCOP2 Family	beta-Galactosidase N-terminal domain-like	8090586	4002476	SCOP2 (2022-06-29)
A	SCOP2 Family	beta-glycanases	8090590	4003164	SCOP2 (2022-06-29)
A	SCOP2 Family	beta-Galactosidase/glucuronidase domain	8090588	4007531	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	E set domains	8090583	3000070	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	E set domains	8090585	3000070	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	galactose-binding domain-like	8090587	3000087	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	(Trans)glycosidases	8090591	3000313	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	beta-Galactosidase/glucuronidase domain-like	8090589	3002047	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	PF02837	e3gm8A2	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF02837	ECOD (1.6)
A	PF00703	e3gm8A3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF00703	ECOD (1.6)
A	PF16355	e3gm8A6	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF16355	ECOD (1.6)
A	PF18565	e3gm8A5	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF18565	ECOD (1.6)
A	PF02836	e3gm8A1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF02836	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
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)
A	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02836	Glycosyl hydrolases family 2, TIM barrel domain (Glyco_hydro_2_C)	Glycosyl hydrolases family 2, TIM barrel domain	This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.	Domain
A	PF00703	Glycosyl hydrolases family 2 (Glyco_hydro_2)	Glycosyl hydrolases family 2	This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.	Domain
A	PF18565	Glycoside hydrolase family 2 C-terminal domain 5 (Glyco_hydro2_C5)	Glycoside hydrolase family 2 C-terminal domain 5	Domain 5 is found in dimeric beta-D-galactosidase from Paracoccus sp. 32d, which contributes to stabilization of the functional dimer. It is suggested that the location of this domain 5, may be one of the factors responsible for the creation of a fun ...	Domain 5 is found in dimeric beta-D-galactosidase from Paracoccus sp. 32d, which contributes to stabilization of the functional dimer. It is suggested that the location of this domain 5, may be one of the factors responsible for the creation of a functional dimer and cold-adaptation of this enzyme [1].	Domain
A	PF02837	Glycosyl hydrolases family 2, sugar binding domain (Glyco_hydro_2_N)	Glycosyl hydrolases family 2, sugar binding domain	This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction.	Domain
A	PF16355	Domain of unknown function (DUF4982) (DUF4982)	Domain of unknown function (DUF4982)	This domain is found towards the C terminus of Beta-glucuronidase from Formosa agariphila (P17_GH2) and similar proteins mainly from bacteria and fungi. P17_GH2 is involved in the degradation of the polysaccharide ulvan. The function of this domain, ...	This domain is found towards the C terminus of Beta-glucuronidase from Formosa agariphila (P17_GH2) and similar proteins mainly from bacteria and fungi. P17_GH2 is involved in the degradation of the polysaccharide ulvan. The function of this domain, which shows an all-beta structure, is unknown [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Glycoside hydrolase family 2, candidate beta-glycosidase	hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity	carbohydrate metabolic process organic substance metabolic process primary metabolic process metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR032311	Domain of unknown function DUF4982	Domain
A	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A	IPR006101	Glycoside hydrolase, family 2	Family
A	IPR040605	Glycoside hydrolase family 2, domain 5	Domain
A	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily
A	IPR006102	Glycoside hydrolase, family 2, immunoglobulin-like beta-sandwich	Domain
A	IPR036156	Beta-Galactosidase/glucuronidase domain superfamily	Homologous Superfamily
A	IPR006104	Glycosyl hydrolases family 2, sugar binding domain	Domain
A	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A	IPR006103	Glycoside hydrolase family 2, catalytic domain	Domain
A	IPR023232	Glycoside hydrolase, family 2, active site	Active Site

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.