Annotations: 1VFN

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1vfna_	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Purine and uridine phosphorylases	Purine and uridine phosphorylases	Purine nucleoside phosphorylase, PNP	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Purine and uridine phosphorylases	8044566	3000626	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	PNP_UDP_1	e1vfnA1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Peptidyl-tRNA hydrolase-like (From Topology)	T: Peptidyl-tRNA hydrolase-like	F: PNP_UDP_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1580	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Nucleoside phosphorylase domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01048	Phosphorylase superfamily (PNP_UDP_1)	Phosphorylase superfamily	Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase)	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PURINE-NUCLEOSIDE PHOSPHORYLASE	guanosine phosphorylase activity pentosyltransferase activity glycosyltransferase activity transferase activity catalytic activity purine-nucleoside phosphorylase activity	glycosyl compound metabolic process carbohydrate derivative metabolic process nucleoside biosynthetic process nucleobase-containing compound metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process small molecule metabolic process cellular metabolic compound salvage purine ribonucleoside metabolic process carbohydrate derivative biosynthetic process glycosyl compound biosynthetic process purine-containing compound salvage small molecule biosynthetic process nucleoside salvage glycosyl compound metabolic process carbohydrate derivative metabolic process nucleoside biosynthetic process nucleobase-containing compound metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process small molecule metabolic process cellular metabolic compound salvage purine ribonucleoside metabolic process carbohydrate derivative biosynthetic process glycosyl compound biosynthetic process purine-containing compound salvage small molecule biosynthetic process nucleoside salvage cellular metabolic process purine ribonucleoside biosynthetic process primary metabolic process ribonucleoside biosynthetic process nucleobase-containing compound biosynthetic process nucleoside metabolic process nucleobase-containing small molecule biosynthetic process purine-containing compound metabolic process purine ribonucleoside salvage biosynthetic process purine nucleoside biosynthetic process metabolic process cellular process purine nucleoside metabolic process ribonucleoside metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR035994	Nucleoside phosphorylase superfamily	Homologous Superfamily
A	IPR011268	Purine nucleoside phosphorylase	Family
A	IPR018099	Purine phosphorylase, family 2, conserved site	Conserved Site
A	IPR011270	Purine nucleoside phosphorylase I, inosine/guanosine-specific	Family
A	IPR000845	Nucleoside phosphorylase domain	Domain

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.