1TZ3

crystal structure of aminoimidazole riboside kinase complexed with aminoimidazole riboside

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1tz3a_	Alpha and beta proteins (a/b)	Ribokinase-like	Ribokinase-like	Ribokinase-like	Aminoimidazole riboside kinase	(Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 ) [TaxId: 99287 ],	SCOPe (2.08)
B	d1tz3b_	Alpha and beta proteins (a/b)	Ribokinase-like	Ribokinase-like	Ribokinase-like	Aminoimidazole riboside kinase	(Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 ) [TaxId: 99287 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Ribokinase-like	8042733	3001268	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Ribokinase-like	8042733	3001268	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	PfkB	e1tz3A1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Ribokinase-like (From Topology)	T: Ribokinase-like	F: PfkB	ECOD (1.6)
B	PfkB	e1tz3B1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Ribokinase-like (From Topology)	T: Ribokinase-like	F: PfkB	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.1190.20	Alpha Beta	3-Layer(aba) Sandwich	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase	Ribokinase	CATH (4.3.0)
B	3.40.1190.20	Alpha Beta	3-Layer(aba) Sandwich	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase	Ribokinase	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	putative sugar kinase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding fructokinase activity carbohydrate kinase activity kinase activity hexokinase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups cation binding metal ion binding	monosaccharide metabolic process carbohydrate metabolic process hexose metabolic process small molecule metabolic process metabolic process cellular process primary metabolic process fructose metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR011611	Carbohydrate kinase PfkB	Domain
A, B	IPR002173	Carbohydrate/purine kinase, PfkB, conserved site	Conserved Site
A, B	IPR029056	Ribokinase-like	Homologous Superfamily
A, B	IPR002139	Ribokinase/fructokinase	Family
A, B	IPR050306	PfkB Carbohydrate Kinase	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	CDP-diacylglycerol diphosphatase M-CSA #751	5-aminoimidazole ribotide (AIR) is a branch point metabolite in the biosynthetic pathways of purines and thiamin. Although AIR cannot be efficiently taken up by most bacteria, 5-aminoimidazole riboside (AIRs) can. Aminoimidazole riboside kinase catalyses the phosphorylation of AIRs into AIR to feed into purine and thiamin biosynthesis pathways.	Defined by 4 residues: GLY:A-269 [auth A-249]ALA:A-270 [auth A-250]GLY:A-271 [auth A-251]ASP:A-272 [auth A-252] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.7.1.4 (PDB Primary Data) Search M-CSA Motif + EC 2.7.1.4 EC: 2.7.1.223 (UniProt) Search M-CSA Motif + EC 2.7.1.223

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.