4AZC

Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Glyco_hydro_20	e4azcB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Glyco_hydro_20	ECOD (1.6)
C	Glyco_hydro_20	e4azcC1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Glyco_hydro_20	ECOD (1.6)
D	Glyco_hydro_20	e4azcD1	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_20	e4azcA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Glyco_hydro_20	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
B	1.20.1270.90	Mainly Alpha	Up-down Bundle	Substrate Binding Domain Of Dnak	Chain:A	CATH (4.3.0)
C	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
C	1.20.1270.90	Mainly Alpha	Up-down Bundle	Substrate Binding Domain Of Dnak	Chain:A	CATH (4.3.0)
D	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
D	1.20.1270.90	Mainly Alpha	Up-down Bundle	Substrate Binding Domain Of Dnak	Chain:A	CATH (4.3.0)
A	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
A	1.20.1270.90	Mainly Alpha	Up-down Bundle	Substrate Binding Domain Of Dnak	Chain:A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B, C, D	PF00728	Glycosyl hydrolase family 20, catalytic domain (Glyco_hydro_20)	Glycosyl hydrolase family 20, catalytic domain	This domain has a TIM barrel 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
B, C, D	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	carbohydrate metabolic process primary metabolic process metabolic process	extracellular region cellular anatomical entity
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	carbohydrate metabolic process primary metabolic process metabolic process	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B, C, D	IPR005877	YSIRK Gram-positive signal peptide	Domain
B, C, D	IPR011098	G5 domain	Domain
B, C, D	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
B, C, D	IPR052764	Glycosyl Hydrolase 20 Enzymes	Family
B, C, D	IPR015883	Glycoside hydrolase family 20, catalytic domain	Domain
B, C, D	IPR019931	LPXTG cell wall anchor domain	Domain
A	IPR005877	YSIRK Gram-positive signal peptide	Domain
A	IPR011098	G5 domain	Domain
A	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A	IPR052764	Glycosyl Hydrolase 20 Enzymes	Family
A	IPR015883	Glycoside hydrolase family 20, catalytic domain	Domain
A	IPR019931	LPXTG cell wall anchor domain	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.