Annotations: 3WIR

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF03636	e3wirA1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: PF03636	ECOD (1.6)
A	PF03633	e3wirA3	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycoside hydrolase family 127 middle domain-related (From Topology)	T: Glycoside hydrolase family 127 middle domain-related	F: PF03633	ECOD (1.6)
A	PF03632	e3wirA2	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: PF03632	ECOD (1.6)
B	PF03636	e3wirB3	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: PF03636	ECOD (1.6)
B	PF03633	e3wirB2	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycoside hydrolase family 127 middle domain-related (From Topology)	T: Glycoside hydrolase family 127 middle domain-related	F: PF03633	ECOD (1.6)
B	PF03632	e3wirB1	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: PF03632	ECOD (1.6)
C	PF03636	e3wirC2	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: PF03636	ECOD (1.6)
C	PF03633	e3wirC3	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycoside hydrolase family 127 middle domain-related (From Topology)	T: Glycoside hydrolase family 127 middle domain-related	F: PF03633	ECOD (1.6)
C	PF03632	e3wirC1	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: PF03632	ECOD (1.6)
D	PF03636	e3wirD1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: PF03636	ECOD (1.6)
D	PF03633	e3wirD3	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycoside hydrolase family 127 middle domain-related (From Topology)	T: Glycoside hydrolase family 127 middle domain-related	F: PF03633	ECOD (1.6)
D	PF03632	e3wirD2	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: PF03632	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.70.98.40	Mainly Beta	Distorted Sandwich	Beta-galactosidase	Chain A, domain 5	CATH (4.3.0)
A	1.50.10.10	Mainly Alpha	Alpha/alpha barrel	Glycosyltransferase		CATH (4.3.0)
A	2.60.420.10	Mainly Beta	Sandwich	Maltose phosphorylase, domain 3	Maltose phosphorylase, domain 3	CATH (4.3.0)
B	2.70.98.40	Mainly Beta	Distorted Sandwich	Beta-galactosidase	Chain A, domain 5	CATH (4.3.0)
B	1.50.10.10	Mainly Alpha	Alpha/alpha barrel	Glycosyltransferase		CATH (4.3.0)
B	2.60.420.10	Mainly Beta	Sandwich	Maltose phosphorylase, domain 3	Maltose phosphorylase, domain 3	CATH (4.3.0)
C	2.70.98.40	Mainly Beta	Distorted Sandwich	Beta-galactosidase	Chain A, domain 5	CATH (4.3.0)
C	1.50.10.10	Mainly Alpha	Alpha/alpha barrel	Glycosyltransferase		CATH (4.3.0)
C	2.60.420.10	Mainly Beta	Sandwich	Maltose phosphorylase, domain 3	Maltose phosphorylase, domain 3	CATH (4.3.0)
D	2.70.98.40	Mainly Beta	Distorted Sandwich	Beta-galactosidase	Chain A, domain 5	CATH (4.3.0)
D	1.50.10.10	Mainly Alpha	Alpha/alpha barrel	Glycosyltransferase		CATH (4.3.0)
D	2.60.420.10	Mainly Beta	Sandwich	Maltose phosphorylase, domain 3	Maltose phosphorylase, domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF03636	Glycosyl hydrolase family 65, N-terminal domain (Glyco_hydro_65N)	Glycosyl hydrolase family 65, N-terminal domain	-	Family
A, B, C, D	PF03632	Glycosyl hydrolase family 65 central catalytic domain (Glyco_hydro_65m)	Glycosyl hydrolase family 65 central catalytic domain	-	Repeat
A, B, C, D	PF03633	Glycosyl hydrolase family 65, C-terminal domain (Glyco_hydro_65C)	Glycosyl hydrolase family 65, C-terminal domain	This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyses the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucos ...	This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyses the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The C-terminal domain forms a two layered jelly roll motif. This domain is situated at the base of the catalytic domain, however its function remains unknown [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Kojibiose phosphorylase	binding carbohydrate binding kojibiose phosphorylase activity glycosyltransferase activity transferase activity glucosyltransferase activity hexosyltransferase 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, B, C, D	IPR012341	Six-hairpin glycosidase-like superfamily	Homologous Superfamily
A, B, C, D	IPR037018	Glycoside hydrolase family 65, N-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR008928	Six-hairpin glycosidase superfamily	Homologous Superfamily
A, B, C, D	IPR005195	Glycoside hydrolase, family 65, central catalytic	Domain
A, B, C, D	IPR017045	Maltose phosphorylase/glycosyl hydrolase/vacuolar acid trehalase	Family
A, B, C, D	IPR011013	Galactose mutarotase-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR005194	Glycoside hydrolase family 65, C-terminal	Domain
A, B, C, D	IPR005196	Glycoside hydrolase, family 65, N-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.