4B1J

Structure of human PARG catalytic domain in complex 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
Pharos: Disease Associations
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4b1ja_	Alpha and beta proteins (a/b)	Macro domain-like	Macro domain-like	Poly(ADP-ribose) glycohydrolase (PARG) catalytic domain-like	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	PARG catalytic domain-like	8046689	4005239	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Macro domain-like	8103588	3000458	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	PF20811	e4b1jA1	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: PF20811	ECOD (1.6)
A	PF05028	e4b1jA2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: PF05028	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	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	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	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	ribose phosphate metabolic process ATP metabolic process carbohydrate derivative metabolic process ATP generation from poly-ADP-D-ribose nucleobase-containing compound metabolic process organic substance 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 ribose phosphate metabolic process ATP metabolic process carbohydrate derivative metabolic process ATP generation from poly-ADP-D-ribose nucleobase-containing compound metabolic process organic substance 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 organonitrogen compound metabolic process cellular metabolic process primary metabolic process nucleotide metabolic process purine-containing compound metabolic process organic cyclic compound metabolic process organophosphate metabolic process metabolic process cellular process macromolecule metabolic process nucleoside triphosphate metabolic process purine ribonucleotide metabolic process carbohydrate metabolic process nucleotide-sugar metabolic process cellular response to stimulus response to stimulus DNA metabolic process base-excision repair, gap-filling nucleic acid metabolic process base-excision repair cellular response to stress DNA damage response response to stress DNA repair 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 regulation of biological process biological regulation regulation of macromolecule metabolic process regulation of DNA repair regulation of response to stimulus regulation of metabolic process regulation of DNA metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nuclear body intracellular organelle nucleoplasm organelle lumen organelle intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nuclear body intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen mitochondrion mitochondrial matrix

InterPro: Protein Family Classification InterPro Database Homepage

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

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q86W56	Embryo Loss

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	CSS	Parent Component: CYS RESID: AA0269 PSI-MOD : L-cysteine persulfide MOD:00274

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.