7A3X

tRNA-guanine transglycosylase C158S/C281S/Y330C/H333A mutant in complex with sulfolane

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
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	d7a3xa_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	tRNA-guanine transglycosylase	tRNA-guanine transglycosylase	Queosine tRNA-guanine transglycosylase	(Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821 ) [TaxId: 264203 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	tRNA-guanine transglycosylase	8040041	3000635	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	TGT	e7a3xA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: TGT	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01702	Queuine tRNA-ribosyltransferase (TGT)	Queuine tRNA-ribosyltransferase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Queuine tRNA-ribosyltransferase	pentosyltransferase activity glycosyltransferase activity catalytic activity, acting on RNA tRNA-guanosine(34) queuine transglycosylase activity catalytic activity, acting on a nucleic acid catalytic activity, acting on a tRNA transferase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	carbohydrate derivative biosynthetic process glycosyl compound metabolic process glycosyl compound biosynthetic process small molecule biosynthetic process carbohydrate derivative metabolic process primary metabolic process ribonucleoside biosynthetic process nucleoside biosynthetic process nucleobase-containing compound biosynthetic process queuosine metabolic process nucleoside metabolic process nucleobase-containing small molecule biosynthetic process nucleobase-containing compound metabolic process queuosine biosynthetic process biosynthetic process carbohydrate derivative biosynthetic process glycosyl compound metabolic process glycosyl compound biosynthetic process small molecule biosynthetic process carbohydrate derivative metabolic process primary metabolic process ribonucleoside biosynthetic process nucleoside biosynthetic process nucleobase-containing compound biosynthetic process queuosine metabolic process nucleoside metabolic process nucleobase-containing small molecule biosynthetic process nucleobase-containing compound metabolic process queuosine biosynthetic process biosynthetic process nucleobase-containing small molecule metabolic process small molecule metabolic process metabolic process ribonucleoside metabolic process cellular biosynthetic process cellular metabolic process tRNA modification RNA metabolic process tRNA-guanine transglycosylation gene expression macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process RNA biosynthetic process nucleic acid biosynthetic process RNA modification tRNA processing macromolecule modification cellular process macromolecule metabolic process RNA processing	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036511	Queuine tRNA-ribosyltransferase-like	Homologous Superfamily
A	IPR004803	tRNA-guanine transglycosylase	Family
A	IPR050076	Archaeosine Synthase Type 1/Queuine TRNA-Ribosyltransferase	Family
A	IPR002616	tRNA-guanine(15) transglycosylase-like	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.