4EWL

Crystal Structure of MshB with glycerol and Acetate bound in the active site

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4ewla_	Alpha and beta proteins (a/b)	LmbE-like	LmbE-like	LmbE-like	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
B	d4ewlb_	Alpha and beta proteins (a/b)	LmbE-like	LmbE-like	LmbE-like	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	LmbE-like	8039834	3000960	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	LmbE-like	8039834	3000960	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	PIG-L	e4ewlA1	A: a/b three-layered sandwiches	X: LmbE-like (From Topology)	H: LmbE-like (From Topology)	T: LmbE-like	F: PIG-L	ECOD (1.6)
B	PIG-L	e4ewlB1	A: a/b three-layered sandwiches	X: LmbE-like (From Topology)	H: LmbE-like (From Topology)	T: LmbE-like	F: PIG-L	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.10320	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	LmbE-like	CATH (4.3.0)
B	3.40.50.10320	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	LmbE-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02585	GlcNAc-PI de-N-acetylase (PIG-L)	GlcNAc-PI de-N-acetylase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase	deacetylase activity N-acetylglucosaminylinositol deacetylase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	carbohydrate derivative biosynthetic process mycothiol biosynthetic process glycosyl compound metabolic process glycosyl compound biosynthetic process cellular biosynthetic process cellular metabolic process glycoside metabolic process carbohydrate derivative metabolic process mycothiol metabolic process glycoside biosynthetic process sulfur compound biosynthetic process biosynthetic process sulfur compound metabolic process metabolic process carbohydrate derivative biosynthetic process mycothiol biosynthetic process glycosyl compound metabolic process glycosyl compound biosynthetic process cellular biosynthetic process cellular metabolic process glycoside metabolic process carbohydrate derivative metabolic process mycothiol metabolic process glycoside biosynthetic process sulfur compound biosynthetic process biosynthetic process sulfur compound metabolic process metabolic process cellular process	cell periphery plasma membrane membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR024078	Putative deacetylase LmbE-like domain superfamily	Homologous Superfamily
A, B	IPR017810	Mycothiol biosynthesis protein, MshB	Family
A, B	IPR003737	N-acetylglucosaminyl phosphatidylinositol deacetylase-related	Family

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.