5MZE

Crystal structure of mouse MTH1 with 8-oxo-dGTP

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	d5mzea_	Alpha and beta proteins (a+b)	Nudix	Nudix	MutT-like	7,8-dihydro-8-oxoguanine triphosphatase Hmth1	House Mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d5mzeb_	Alpha and beta proteins (a+b)	Nudix	Nudix	MutT-like	7,8-dihydro-8-oxoguanine triphosphatase Hmth1	House Mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
C	d5mzec_	Alpha and beta proteins (a+b)	Nudix	Nudix	MutT-like	7,8-dihydro-8-oxoguanine triphosphatase Hmth1	House Mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
D	d5mzed_	Alpha and beta proteins (a+b)	Nudix	Nudix	MutT-like	7,8-dihydro-8-oxoguanine triphosphatase Hmth1	House 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)
A	SCOP2B Superfamily	Nudix	8058796	3000098	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Nudix	8058796	3000098	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Nudix	8058796	3000098	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Nudix	8058796	3000098	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	PF00293	e5mzeA1	A: a+b two layers	X: beta-Grasp	H: Nudix (From Topology)	T: Nudix	F: PF00293	ECOD (1.6)
B	PF00293	e5mzeB1	A: a+b two layers	X: beta-Grasp	H: Nudix (From Topology)	T: Nudix	F: PF00293	ECOD (1.6)
C	PF00293	e5mzeC1	A: a+b two layers	X: beta-Grasp	H: Nudix (From Topology)	T: Nudix	F: PF00293	ECOD (1.6)
D	PF00293	e5mzeD1	A: a+b two layers	X: beta-Grasp	H: Nudix (From Topology)	T: Nudix	F: PF00293	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.79.10	Alpha Beta	Alpha-Beta Complex	Nucleoside Triphosphate Pyrophosphohydrolase	Nucleoside Triphosphate Pyrophosphohydrolase	CATH (4.3.0)
B	3.90.79.10	Alpha Beta	Alpha-Beta Complex	Nucleoside Triphosphate Pyrophosphohydrolase	Nucleoside Triphosphate Pyrophosphohydrolase	CATH (4.3.0)
C	3.90.79.10	Alpha Beta	Alpha-Beta Complex	Nucleoside Triphosphate Pyrophosphohydrolase	Nucleoside Triphosphate Pyrophosphohydrolase	CATH (utative)
D	3.90.79.10	Alpha Beta	Alpha-Beta Complex	Nucleoside Triphosphate Pyrophosphohydrolase	Nucleoside Triphosphate Pyrophosphohydrolase	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00293	NUDIX domain (NUDIX)	NUDIX domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	7,8-dihydro-8-oxoguanine triphosphatase	RNA binding binding organic cyclic compound binding snoRNA binding nucleic acid binding O6-methyl-dGTP hydrolase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity pyrophosphatase activity 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity nucleoside triphosphate diphosphatase activity ATP diphosphatase activity RNA binding binding organic cyclic compound binding snoRNA binding nucleic acid binding O6-methyl-dGTP hydrolase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity pyrophosphatase activity 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity nucleoside triphosphate diphosphatase activity ATP diphosphatase activity N6-methyl-(d)ATP hydrolase activity 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity 2-hydroxy-ATP hydrolase activity dATP diphosphatase activity 2-hydroxy-dATP hydrolase activity cation binding ion binding metal ion binding small molecule binding	developmental process multicellular organismal process gonad development reproductive system development reproductive process sex differentiation animal organ development developmental process involved in reproduction male gonad development male sex differentiation multicellular organism development development of primary male sexual characteristics development of primary sexual characteristics anatomical structure development reproductive structure development developmental process multicellular organismal process gonad development reproductive system development reproductive process sex differentiation animal organ development developmental process involved in reproduction male gonad development male sex differentiation multicellular organism development development of primary male sexual characteristics development of primary sexual characteristics anatomical structure development reproductive structure development system development glycosyl compound metabolic process catabolic process purine nucleoside catabolic process carbohydrate derivative metabolic process nucleobase-containing compound metabolic process organic substance metabolic process nucleobase-containing small molecule metabolic process small molecule metabolic process organonitrogen compound catabolic process carbohydrate derivative catabolic process organonitrogen compound metabolic process primary metabolic process glycosyl compound catabolic process purine-containing compound catabolic process nucleoside metabolic process organic cyclic compound catabolic process nucleobase-containing compound catabolic process purine-containing compound metabolic process organic cyclic compound metabolic process nucleobase-containing small molecule catabolic process nucleoside catabolic process metabolic process small molecule catabolic process organic substance catabolic process purine nucleoside metabolic process response to stimulus response to metal ion response to chemical response to cadmium ion response to inorganic substance cellular response to stimulus DNA metabolic process nucleic acid metabolic process cellular response to stress response to stress cellular process macromolecule metabolic process DNA protection	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle nuclear membrane membrane nucleus endomembrane system organelle envelope nuclear envelope membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle nuclear membrane membrane nucleus endomembrane system organelle envelope nuclear envelope organelle membrane cytosol extracellular region extracellular space membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen acrosomal vesicle intracellular vesicle cytoplasmic vesicle secretory granule secretory vesicle vesicle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR015797	NUDIX hydrolase-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR003563	Oxidized purine nucleoside triphosphate	Family
A, B, C, D	IPR000086	NUDIX hydrolase domain	Domain
A, B, C, D	IPR020084	NUDIX hydrolase, conserved site	Conserved Site
A, B, C, D	IPR020476	NUDIX hydrolase	Domain

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.