Annotations: 1IBS

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ibsa1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	Phosphoribosylpyrophosphate synthetase-like	Phosphoribosylpyrophosphate synthetase	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)
B	d1ibsb1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	Phosphoribosylpyrophosphate synthetase-like	Phosphoribosylpyrophosphate synthetase	(Bacillus subtilis ) [TaxId: 1423 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	PRTase-like	8032251	3000060	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	PRTase-like	8032253	3000060	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	PRTase-like	8032253	3000060	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	PRTase-like	8032251	3000060	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	Pribosyltran_N	e1ibsA1	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyltran_N	ECOD (1.6)
A	Pribosyl_synth	e1ibsA2	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyl_synth	ECOD (1.6)
B	Pribosyltran_N	e1ibsB1	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyltran_N	ECOD (1.6)
B	Pribosyl_synth	e1ibsB2	A: a/b three-layered sandwiches	X: PRTase-like (From Topology)	H: PRTase-like (From Topology)	T: PRTase-like	F: Pribosyl_synth	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF14572	Phosphoribosyl synthetase-associated domain (Pribosyl_synth)	Phosphoribosyl synthetase-associated domain	This family includes several examples of enzymes from class EC:2.7.6.1, phosphoribosyl-pyrophosphate transferase.	Domain
A, B	PF13793	N-terminal domain of ribose phosphate pyrophosphokinase (Pribosyltran_N)	N-terminal domain of ribose phosphate pyrophosphokinase	This family is frequently found N-terminal to the Pribosyltran, Pfam:PF00156.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	RIBOSE-PHOSPHATE PYROPHOSPHOKINASE	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding kinase activity transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups ribose phosphate diphosphokinase activity diphosphotransferase activity	nucleotide biosynthetic process organonitrogen compound biosynthetic process nucleobase-containing compound metabolic process purine nucleotide metabolic process organic substance metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process organic substance biosynthetic process small molecule metabolic process phosphorus metabolic process nucleoside phosphate metabolic process organonitrogen compound metabolic process cellular metabolic process nucleotide biosynthetic process organonitrogen compound biosynthetic process nucleobase-containing compound metabolic process purine nucleotide metabolic process organic substance metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process organic substance biosynthetic process small molecule metabolic process phosphorus metabolic process nucleoside phosphate metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process organic cyclic compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process organic cyclic compound biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process purine nucleotide biosynthetic process ribonucleoside monophosphate metabolic process nucleoside monophosphate metabolic process nucleoside monophosphate biosynthetic process ribonucleoside monophosphate biosynthetic process 5-phosphoribose 1-diphosphate biosynthetic process ribose phosphate metabolic process carbohydrate derivative biosynthetic process carbohydrate derivative metabolic process 5-phosphoribose 1-diphosphate metabolic process ribose phosphate biosynthetic process phosphorylation	ribose phosphate diphosphokinase complex transferase complex, transferring phosphorus-containing groups protein-containing complex catalytic complex transferase complex intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR000842	Phosphoribosyl pyrophosphate synthetase, conserved site	Conserved Site
A, B	IPR000836	Phosphoribosyltransferase domain	Domain
A, B	IPR037515	Ribose-phosphate pyrophosphokinase, bacterial-type	Family
A, B	IPR029057	Phosphoribosyltransferase-like	Homologous Superfamily
A, B	IPR029099	Ribose-phosphate pyrophosphokinase, N-terminal domain	Domain
A, B	IPR005946	Ribose-phosphate pyrophosphokinase	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.