2PYU

Structure of the E. coli inosine triphosphate pyrophosphatase RgdB in complex with IMP

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	d2pyua1	Alpha and beta proteins (a/b)	Anticodon-binding domain-like	ITPase-like	automated matches	automated matches	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
A	d2pyua2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	ITPase-like	8058165	3000497	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	PF01725	e2pyuA1	A: a/b three-layered sandwiches	X: ITPase-like (From Topology)	H: ITPase-like (From Topology)	T: ITPase-like	F: PF01725	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.950.10	Alpha Beta	Alpha-Beta Complex	Maf protein		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01725	Ham1 family (Ham1p_like)	Ham1 family	This family consists of the HAM1 protein Swiss:P47119 and hypothetical archaeal bacterial and C. elegans proteins. HAM1 controls 6-N-hydroxylaminopurine (HAP) sensitivity and mutagenesis in S. cerevisiae Swiss:P47119 [1]. The HAM1 protein protects th ...	This family consists of the HAM1 protein Swiss:P47119 and hypothetical archaeal bacterial and C. elegans proteins. HAM1 controls 6-N-hydroxylaminopurine (HAP) sensitivity and mutagenesis in S. cerevisiae Swiss:P47119 [1]. The HAM1 protein protects the cell from HAP, either on the level of deoxynucleoside triphosphate or the DNA level by a yet unidentified set of reactions [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Inosine Triphosphate Pyrophosphatase RdgB	pyrophosphatase activity ITP diphosphatase activity nucleoside triphosphate diphosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding dITP diphosphatase activity pyrophosphatase activity ITP diphosphatase activity nucleoside triphosphate diphosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding dITP diphosphatase activity identical protein binding protein binding protein homodimerization activity protein dimerization activity ribonucleoside triphosphate phosphatase activity XTP diphosphatase activity nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding	catabolic process nucleoside triphosphate catabolic process purine nucleoside triphosphate catabolic process organophosphate catabolic process nucleoside phosphate catabolic process nucleobase-containing compound metabolic process organic substance metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process small molecule metabolic process phosphorus metabolic process purine nucleoside triphosphate metabolic process nucleoside phosphate metabolic process cellular metabolic process catabolic process nucleoside triphosphate catabolic process purine nucleoside triphosphate catabolic process organophosphate catabolic process nucleoside phosphate catabolic process nucleobase-containing compound metabolic process organic substance metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process small molecule metabolic process phosphorus metabolic process purine nucleoside triphosphate metabolic process nucleoside phosphate metabolic process cellular metabolic process primary metabolic process organic cyclic compound catabolic process nucleobase-containing compound catabolic process organic cyclic compound metabolic process organophosphate metabolic process metabolic process cellular process nucleoside triphosphate metabolic process organic substance catabolic process nucleotide metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR029001	Inosine triphosphate pyrophosphatase-like	Homologous Superfamily
A	IPR020922	dITP/XTP pyrophosphatase	Family
A	IPR002637	RdgB/HAM1	Family

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.