1JAK

Streptomyces plicatus beta-N-acetylhexosaminidase in Complex with (2R,3R,4S,5R)-2-acetamido-3,4-dihydroxy-5-hydroxymethyl-piperidinium chloride (IFG)

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	d1jaka1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	beta-N-acetylhexosaminidase catalytic domain	beta-N-acetylhexosaminidase	(Streptomyces plicatus ) [TaxId: 1922 ],	SCOPe (2.08)
A	d1jaka2	Alpha and beta proteins (a+b)	Zincin-like	beta-N-acetylhexosaminidase-like domain	beta-N-acetylhexosaminidase domain	beta-N-acetylhexosaminidase, N-terminal domain	(Streptomyces plicatus ) [TaxId: 1922 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	beta-N-acetylhexosaminidase catalytic domain	8024476	4003199	SCOP2 (2022-06-29)
A	SCOP2 Family	beta-N-acetylhexosaminidase domain	8024478	4001646	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	(Trans)glycosidases	8036855	3000313	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	beta-N-acetylhexosaminidase-like domain	8036857	3000192	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	Glyco_hydro_20	e1jakA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Glyco_hydro_20	ECOD (1.6)
A	Glyco_hydro_20b	e1jakA2	A: mixed a+b and a/b	X: Zincin-like	H: beta-N-acetylhexosaminidase-like domain (From Topology)	T: beta-N-acetylhexosaminidase-like domain	F: Glyco_hydro_20b	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)
A	3.30.379.10	Alpha Beta	2-Layer Sandwich	Chitobiase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02838	Glycosyl hydrolase family 20, domain 2 (Glyco_hydro_20b)	Glycosyl hydrolase family 20, domain 2	This domain has a zincin-like fold.	Domain
A	PF00728	Glycosyl hydrolase family 20, catalytic domain (Glyco_hydro_20)	Glycosyl hydrolase family 20, catalytic domain	This domain has a TIM barrel fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Beta-N-acetylhexosaminidase	hydrolase activity, acting on glycosyl bonds hexosaminidase activity beta-N-acetylhexosaminidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity	glycosaminoglycan metabolic process aminoglycan metabolic process carbohydrate derivative metabolic process metabolic process cellular process macromolecule metabolic process carbohydrate metabolic process primary metabolic process	cellular anatomical structure membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A	IPR029018	Beta-hexosaminidase-like, domain 2	Homologous Superfamily
A	IPR015883	Glycoside hydrolase family 20, catalytic domain	Domain
A	IPR025705	Beta-hexosaminidase	Family
A	IPR015882	Beta-hexosaminidase, bacterial type, N-terminal	Domain

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.