2CJE

THE CRYSTAL STRUCTURE OF A COMPLEX OF Leishmania major DUTPASE WITH SUBSTRATE ANALOGUE DUPNHP

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	d2cjea_	All alpha proteins	all-alpha NTP pyrophosphatases	all-alpha NTP pyrophosphatases	automated matches	automated matches	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	all-alpha NTP pyrophosphatases	8062837	3001174	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	dUTPase_2	e2cjeA1	A: alpha bundles	X: all-alpha NTP pyrophosphatases (From Homology)	H: all-alpha NTP pyrophosphatases	T: Type II deoxyuridine triphosphatase-related	F: dUTPase_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.1680.10	Mainly Alpha	Up-down Bundle	all-alpha NTP pyrophosphatases	Type II deoxyuridine triphosphatase	CATH (4.3.0)
A	1.20.1670.10	Mainly Alpha	Up-down Bundle	all-alpha NTP pyrophosphatase	Type II deoxyuridine triphosphatase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF08761	dUTPase (dUTPase_2)	dUTPase	2-Deoxyuridine 5-triphosphate nucleotidohydrolase (dUTPase) catalyses the hydrolysis of dUTP to dUMP and pyrophosphate (EC:3.6.1.23). Members of this family have a novel all-alpha fold and are unrelated to the all-beta fold found in dUTPases of the ...	2-Deoxyuridine 5-triphosphate nucleotidohydrolase (dUTPase) catalyses the hydrolysis of dUTP to dUMP and pyrophosphate (EC:3.6.1.23). Members of this family have a novel all-alpha fold and are unrelated to the all-beta fold found in dUTPases of the majority of organisms [1]. This family contains both dUTPase homologues of dUTPase including dCTPase of phage T4.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	DUTPASE	pyrophosphatase activity nucleoside triphosphate diphosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides dUTP diphosphatase activity hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity cation binding ion binding binding metal ion binding small molecule binding	-	membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR014871	dUTPase/dCTP pyrophosphatase	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.