4NA4

Crystal structure of mouse poly(ADP-ribose) glycohydrolase (PARG) catalytic domain with ADP-HPD

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
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)
C	d4na4c_	Alpha and beta proteins (a/b)	Macro domain-like	Macro domain-like	Poly(ADP-ribose) glycohydrolase (PARG) catalytic domain-like	Poly(ADP-ribose) glycohydrolase (PARG) catalytic domain	mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
A	d4na4a_	Alpha and beta proteins (a/b)	Macro domain-like	Macro domain-like	Poly(ADP-ribose) glycohydrolase (PARG) catalytic domain-like	Poly(ADP-ribose) glycohydrolase (PARG) catalytic domain	mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d4na4b_	Alpha and beta proteins (a/b)	Macro domain-like	Macro domain-like	Poly(ADP-ribose) glycohydrolase (PARG) catalytic domain-like	Poly(ADP-ribose) glycohydrolase (PARG) catalytic domain	mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	Macro domain-like	8103585	3000458	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Macro domain-like	8103585	3000458	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Macro domain-like	8103585	3000458	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)
C	PARG_cat_N	e4na4C1	A: alpha arrays	X: Poly(ADP-ribose) glycohydrolase helical domain (From Topology)	H: Poly(ADP-ribose) glycohydrolase helical domain (From Topology)	T: Poly(ADP-ribose) glycohydrolase helical domain	F: PARG_cat_N	ECOD (1.6)
C	PARG_cat_C	e4na4C2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: PARG_cat_C	ECOD (1.6)
A	PARG_cat_N	e4na4A1	A: alpha arrays	X: Poly(ADP-ribose) glycohydrolase helical domain (From Topology)	H: Poly(ADP-ribose) glycohydrolase helical domain (From Topology)	T: Poly(ADP-ribose) glycohydrolase helical domain	F: PARG_cat_N	ECOD (1.6)
A	PARG_cat_C	e4na4A2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: PARG_cat_C	ECOD (1.6)
B	PARG_cat_N	e4na4B1	A: alpha arrays	X: Poly(ADP-ribose) glycohydrolase helical domain (From Topology)	H: Poly(ADP-ribose) glycohydrolase helical domain (From Topology)	T: Poly(ADP-ribose) glycohydrolase helical domain	F: PARG_cat_N	ECOD (1.6)
B	PARG_cat_C	e4na4B2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: PARG_cat_C	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF05028	Poly (ADP-ribose) glycohydrolase (PARG), Macro domain fold (PARG_cat_C)	Poly (ADP-ribose) glycohydrolase (PARG), Macro domain fold	Poly(ADP-ribose) glycohydrolase (PARG), is a ubiquitously expressed exo- and endoglycohydrolase which mediates oxidative and excitotoxic neuronal death [1]. It catalyses hydrolysis of the O-glycosidic linkages of ADP-ribose polymers, which reverses t ...	Poly(ADP-ribose) glycohydrolase (PARG), is a ubiquitously expressed exo- and endoglycohydrolase which mediates oxidative and excitotoxic neuronal death [1]. It catalyses hydrolysis of the O-glycosidic linkages of ADP-ribose polymers, which reverses the effects of poly(ADP-ribose) [2,3]. This entry represents the Macro domain fold localised in the C-terminal end of PARG catalytic domain from animals and plants [2,3].	Domain
A, B, C	PF20811	Poly (ADP-ribose) glycohydrolase (PARG), helical domain (PARG_cat_N)	Poly (ADP-ribose) glycohydrolase (PARG), helical domain	Poly(ADP-ribose) glycohydrolase (PARG), is a ubiquitously expressed exo- and endoglycohydrolase which mediates oxidative and excitotoxic neuronal death [1]. It catalyses hydrolysis of the O-glycosidic linkages of ADP-ribose polymers, which reverses t ...	Poly(ADP-ribose) glycohydrolase (PARG), is a ubiquitously expressed exo- and endoglycohydrolase which mediates oxidative and excitotoxic neuronal death [1]. It catalyses hydrolysis of the O-glycosidic linkages of ADP-ribose polymers, which reverses the effects of poly(ADP-ribose) [2,3]. This entry represents the helical domain of PARG catalytic domain from animals and plants, found at the N-terminal of PARG catalytic domain [2,3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Poly(ADP-ribose) glycohydrolase	hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity poly(ADP-ribose) glycohydrolase activity catalytic activity	cellular response to stimulus cellular response to stress response to stimulus DNA damage response response to stress cellular process ribose phosphate metabolic process ATP metabolic process carbohydrate derivative metabolic process ATP generation from poly-ADP-D-ribose nucleobase-containing compound metabolic process purine nucleotide metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process cellular response to stimulus cellular response to stress response to stimulus DNA damage response response to stress cellular process ribose phosphate metabolic process ATP metabolic process carbohydrate derivative metabolic process ATP generation from poly-ADP-D-ribose nucleobase-containing compound metabolic process purine nucleotide metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process purine ribonucleoside triphosphate metabolic process phosphate-containing compound metabolic process small molecule metabolic process phosphorus metabolic process ribonucleoside triphosphate metabolic process nucleoside phosphate metabolic process purine nucleoside triphosphate metabolic process primary metabolic process nucleotide metabolic process purine-containing compound metabolic process organophosphate metabolic process metabolic process macromolecule metabolic process nucleoside triphosphate metabolic process purine ribonucleotide metabolic process biological process involved in interspecies interaction between organisms detection of external biotic stimulus response to other organism response to external stimulus detection of biotic stimulus detection of bacterium response to biotic stimulus detection of stimulus response to bacterium detection of other organism response to external biotic stimulus carbohydrate metabolic process regulation of cellular process regulation of cellular response to stress regulation of primary metabolic process regulation of response to stress regulation of nucleobase-containing compound metabolic process DNA repair regulation of biological process biological regulation DNA metabolic process regulation of macromolecule metabolic process nucleic acid metabolic process regulation of DNA repair regulation of response to stimulus regulation of metabolic process regulation of DNA metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR048362	Poly (ADP-ribose) glycohydrolase, helical domain	Domain
A, B, C	IPR046372	Poly (ADP-ribose) glycohydrolase (PARG), catalytic domain	Domain
A, B, C	IPR007724	Poly(ADP-ribose) glycohydrolase	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.