7DSR

Anthranilate phosphoribosyltransferase variant Gly141Asn from Saccharomyces cerevisiae in complex with 4-fluoroanthranilate

External Resource: Annotation

Domain Annotation: ECOD Classification
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	F_UNCLASSIFIED	e7dsrA2	A: alpha arrays	X: Nucleoside phosphorylase/phosphoribosyltransferase-N (From Topology)	H: Nucleoside phosphorylase/phosphoribosyltransferase-N (From Topology)	T: Nucleoside phosphorylase/phosphoribosyltransferase-N	F: F_UNCLASSIFIED	ECOD (1.6)
A	Glycos_transf_3	e7dsrA1	A: a/b three-layered sandwiches	X: Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain (From Topology)	H: Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain (From Topology)	T: Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain	F: Glycos_transf_3	ECOD (1.6)
B	F_UNCLASSIFIED	e7dsrB2	A: alpha arrays	X: Nucleoside phosphorylase/phosphoribosyltransferase-N (From Topology)	H: Nucleoside phosphorylase/phosphoribosyltransferase-N (From Topology)	T: Nucleoside phosphorylase/phosphoribosyltransferase-N	F: F_UNCLASSIFIED	ECOD (1.6)
B	Glycos_transf_3	e7dsrB1	A: a/b three-layered sandwiches	X: Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain (From Topology)	H: Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain (From Topology)	T: Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain	F: Glycos_transf_3	ECOD (1.6)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Anthranilate phosphoribosyltransferase	pentosyltransferase activity glycosyltransferase activity transferase activity anthranilate phosphoribosyltransferase activity catalytic activity	oxoacid metabolic process cellular biosynthetic process indole-containing compound metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process biogenic amine biosynthetic process tryptophan biosynthetic process indole-containing compound biosynthetic process indolalkylamine metabolic process small molecule metabolic process indolalkylamine biosynthetic process oxoacid metabolic process cellular biosynthetic process indole-containing compound metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process biogenic amine biosynthetic process tryptophan biosynthetic process indole-containing compound biosynthetic process indolalkylamine metabolic process small molecule metabolic process indolalkylamine biosynthetic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process primary metabolic process amine metabolic process amino acid biosynthetic process biosynthetic process amine biosynthetic process metabolic process cellular process biogenic amine metabolic process alpha-amino acid biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR035902	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain superfamily	Homologous Superfamily
A, B	IPR000312	Glycosyl transferase, family 3	Domain
A, B	IPR005940	Anthranilate phosphoribosyl transferase	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.