1MYR

MYROSINASE FROM SINAPIS ALBA

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1myra_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	Family 1 of glycosyl hydrolase	Plant beta-glucosidase (myrosinase)	(Sinapis alba ) [TaxId: 3728 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	(Trans)glycosidases	8032543	3000313	SCOP2B (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	Glyco_hydro_1	e1myrA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Glyco_hydro_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
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	PF00232	Glycosyl hydrolase family 1 (Glyco_hydro_1)	Glycosyl hydrolase family 1		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	MYROSINASE	hydrolase activity, acting on glycosyl bonds glucosidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity beta-glucosidase activity catalytic activity thioglucosidase activity cation binding ion binding binding metal ion binding small molecule binding	carbohydrate metabolic process primary metabolic process metabolic process cellular process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle vacuole cytoplasm intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001360	Glycoside hydrolase family 1	Family
A	IPR018120	Glycoside hydrolase family 1, active site	Active Site
A	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A	IPR033132	Glycosyl hydrolases family 1, N-terminal conserved site	Conserved Site

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	thioglucosidase M-CSA #460	Myronase is the enzyme responsible for the hydrolysis of a variety of plant anionic-1-thio-beta-glucosides, called glucosinolates. Sinapsis alba myrosinase is a 499 amino acid S-glucosidase which hydrolyses an S-glycosidic bond, and is closely related to the O-glucosidases. Upon hydrolysis, configuration at the anomeric centre is retained. Myrosinases are thought to be involved in defence systems developed by plants The protein fold into a (beta/alpha)8 barrel structure, forming a dimer which is stabilised by a Zn ion, and is heavily glycosylated. It is a member of the glycoside hydrolase family 1 (GH1).	Defined by 6 residues: ARG:A-95GLN:A-187SER:A-190ASN:A-328TYR:A-330GLU:A-409 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.2.3.1 (PDB Primary Data) Search M-CSA Motif + EC 3.2.3.1 EC: 3.2.1.147 (UniProt) Search M-CSA Motif + EC 3.2.1.147

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 R01GM157729.