3MBI

Crystal structure of the phosphoribosylpyrophosphate (PRPP) synthetase from Thermoplasma volcanium in complex with ADP-Mg2+ and ribose 5-phosphate

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d3mbia1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	automated matches	automated matches	(Thermoplasma volcanium ) [TaxId: 50339 ],	SCOPe (2.08)
A	d3mbia3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Thermoplasma volcanium ) [TaxId: 50339 ],	SCOPe (2.08)
B	d3mbib1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	automated matches	automated matches	(Thermoplasma volcanium ) [TaxId: 50339 ],	SCOPe (2.08)
B	d3mbib3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Thermoplasma volcanium ) [TaxId: 50339 ],	SCOPe (2.08)
C	d3mbic1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	automated matches	automated matches	(Thermoplasma volcanium ) [TaxId: 50339 ],	SCOPe (2.08)
D	d3mbid1	Alpha and beta proteins (a/b)	PRTase-like	PRTase-like	automated matches	automated matches	(Thermoplasma volcanium ) [TaxId: 50339 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Pribosyltran_N	e3mbiA3	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	e3mbiA2	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	e3mbiB3	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	e3mbiB2	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)
C	Pribosyltran_N	e3mbiC3	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)
C	Pribosyl_synth	e3mbiC2	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)
D	Pribosyltran_N	e3mbiD3	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)
D	Pribosyl_synth	e3mbiD2	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)
C	3.40.50.2020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
D	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, C, D	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
A, B, C, D	PF00156	Phosphoribosyl transferase domain (Pribosyltran)	Phosphoribosyl transferase domain	This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7, Swiss:P07672. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase Swiss:P51900. Hypoxanthine phosph ...	This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7, Swiss:P07672. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase Swiss:P51900. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8 Swiss:P36766. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1 Swiss:P09329. Amidophosphoribosyltransferase EC:2.4.2.14 Swiss:P00496. Orotate phosphoribosyl-transferase EC:2.4.2.10 Swiss:P11172. Uracil phosphoribosyl-transferase EC:2.4.2.9 Swiss:P25532. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22 Swiss:P00501. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	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	nucleoside phosphate metabolic process cellular metabolic process nucleotide biosynthetic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process biosynthetic process organophosphate metabolic process nucleobase-containing small molecule metabolic process organophosphate biosynthetic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process nucleoside phosphate metabolic process cellular metabolic process nucleotide biosynthetic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process biosynthetic process organophosphate metabolic process nucleobase-containing small molecule metabolic process organophosphate biosynthetic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process nucleoside phosphate biosynthetic process metabolic process cellular process small molecule metabolic process phosphorus metabolic process purine nucleotide 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	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, C, D	IPR000836	Phosphoribosyltransferase domain	Domain
A, B, C, D	IPR029057	Phosphoribosyltransferase-like	Homologous Superfamily
A, B, C, D	IPR029099	Ribose-phosphate pyrophosphokinase, N-terminal domain	Domain
A, B, C, D	IPR005946	Ribose-phosphate pyrophosphokinase	Family
A, B, C, D	IPR037514	Ribose-phosphate pyrophosphokinase, archaea	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.