2J4E

THE ITP COMPLEX OF HUMAN INOSINE TRIPHOSPHATASE

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2j4ea_	Alpha and beta proteins (a/b)	Anticodon-binding domain-like	ITPase-like	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2j4eb_	Alpha and beta proteins (a/b)	Anticodon-binding domain-like	ITPase-like	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d2j4ec_	Alpha and beta proteins (a/b)	Anticodon-binding domain-like	ITPase-like	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d2j4ed2	Alpha and beta proteins (a/b)	Anticodon-binding domain-like	ITPase-like	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d2j4ed3	Artifacts	Tags	Tags	Tags	N-terminal Tags	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d2j4ee_	Alpha and beta proteins (a/b)	Anticodon-binding domain-like	ITPase-like	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d2j4ef_	Alpha and beta proteins (a/b)	Anticodon-binding domain-like	ITPase-like	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
G	d2j4eg_	Alpha and beta proteins (a/b)	Anticodon-binding domain-like	ITPase-like	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
H	d2j4eh_	Alpha and beta proteins (a/b)	Anticodon-binding domain-like	ITPase-like	automated matches	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	SCOP2B Superfamily	ITPase-like	8017421	3000497	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	ITPase-like	8017421	3000497	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	ITPase-like	8017421	3000497	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	ITPase-like	8017421	3000497	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	ITPase-like	8017421	3000497	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	ITPase-like	8017421	3000497	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	ITPase-like	8017421	3000497	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	ITPase-like	8017421	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	Ham1p_like	e2j4eA1	A: a/b three-layered sandwiches	X: ITPase-like (From Topology)	H: ITPase-like (From Topology)	T: ITPase-like	F: Ham1p_like	ECOD (1.6)
B	Ham1p_like	e2j4eB1	A: a/b three-layered sandwiches	X: ITPase-like (From Topology)	H: ITPase-like (From Topology)	T: ITPase-like	F: Ham1p_like	ECOD (1.6)
C	Ham1p_like	e2j4eC1	A: a/b three-layered sandwiches	X: ITPase-like (From Topology)	H: ITPase-like (From Topology)	T: ITPase-like	F: Ham1p_like	ECOD (1.6)
D	Ham1p_like	e2j4eD1	A: a/b three-layered sandwiches	X: ITPase-like (From Topology)	H: ITPase-like (From Topology)	T: ITPase-like	F: Ham1p_like	ECOD (1.6)
E	Ham1p_like	e2j4eE1	A: a/b three-layered sandwiches	X: ITPase-like (From Topology)	H: ITPase-like (From Topology)	T: ITPase-like	F: Ham1p_like	ECOD (1.6)
F	Ham1p_like	e2j4eF1	A: a/b three-layered sandwiches	X: ITPase-like (From Topology)	H: ITPase-like (From Topology)	T: ITPase-like	F: Ham1p_like	ECOD (1.6)
G	Ham1p_like	e2j4eG1	A: a/b three-layered sandwiches	X: ITPase-like (From Topology)	H: ITPase-like (From Topology)	T: ITPase-like	F: Ham1p_like	ECOD (1.6)
H	Ham1p_like	e2j4eH1	A: a/b three-layered sandwiches	X: ITPase-like (From Topology)	H: ITPase-like (From Topology)	T: ITPase-like	F: Ham1p_like	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)
B	3.90.950.10	Alpha Beta	Alpha-Beta Complex	Maf protein		CATH (4.3.0)
C	3.90.950.10	Alpha Beta	Alpha-Beta Complex	Maf protein		CATH (4.3.0)
D	3.90.950.10	Alpha Beta	Alpha-Beta Complex	Maf protein		CATH (4.3.0)
E	3.90.950.10	Alpha Beta	Alpha-Beta Complex	Maf protein		CATH (4.3.0)
F	3.90.950.10	Alpha Beta	Alpha-Beta Complex	Maf protein		CATH (4.3.0)
G	3.90.950.10	Alpha Beta	Alpha-Beta Complex	Maf protein		CATH (4.3.0)
H	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, B, C, D, E A, B, C, D, E, F, G, H	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, B, C, D, E A, B, C, D, E, F, G, H	INOSINE TRIPHOSPHATE PYROPHOSPHATASE	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 dITP diphosphatase activity XTP diphosphatase activity binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding 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 dITP diphosphatase activity XTP diphosphatase activity binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding cation binding ion binding metal ion binding identical protein binding protein binding	nucleoside phosphate metabolic process catabolic process nucleoside triphosphate catabolic process organophosphate catabolic process primary metabolic process deoxyribonucleoside triphosphate catabolic process nucleoside phosphate catabolic process nucleobase-containing compound catabolic process nucleobase-containing compound metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process nucleoside phosphate metabolic process catabolic process nucleoside triphosphate catabolic process organophosphate catabolic process primary metabolic process deoxyribonucleoside triphosphate catabolic process nucleoside phosphate catabolic process nucleobase-containing compound catabolic process nucleobase-containing compound metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process cellular process small molecule metabolic process nucleoside triphosphate metabolic process phosphorus metabolic process deoxyribonucleoside triphosphate metabolic process cellular component organization organelle organization chromosome organization cellular component organization or biogenesis ribose phosphate metabolic process ribonucleotide catabolic process purine ribonucleoside triphosphate catabolic process purine nucleoside triphosphate catabolic process carbohydrate derivative metabolic process ribonucleoside triphosphate catabolic process purine nucleotide metabolic process ribonucleotide metabolic process purine ribonucleoside triphosphate metabolic process purine ribonucleotide catabolic process ribonucleoside triphosphate metabolic process nucleotide catabolic process purine nucleoside triphosphate metabolic process purine nucleotide catabolic process ITP catabolic process carbohydrate derivative catabolic process purine-containing compound catabolic process nucleotide metabolic process purine-containing compound metabolic process ITP metabolic process purine ribonucleotide metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle organelle intracellular membrane-bounded organelle nucleus membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR029001	Inosine triphosphate pyrophosphatase-like	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR027502	Inosine triphosphate pyrophosphatase	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR002637	RdgB/HAM1	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F, G, H	Pharos: Q9BY32	developmental and epileptic encephalopathy, 35 inosine triphosphatase deficiency thrombocytopenia inborn errors of metabolism hemolytic anemia Anemia, Hemolytic glioblastoma lung cancer epilepsy hepatitis C virus infection intellectual disability psoriasis

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.