1XJN

Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP-CDP complex

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
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	Ribonuc_red_lgN_1	e1xjnA2	A: alpha arrays	X: RuvA-C	H: ATP cone (From Topology)	T: ATP cone	F: Ribonuc_red_lgN_1	ECOD (1.6)
A	Ribonuc_red_lgC	e1xjnA1	A: a/b barrels	X: Ten stranded beta/alpha barrel (From Topology)	H: Ten stranded beta/alpha barrel (From Topology)	T: Ten stranded beta/alpha barrel	F: Ribonuc_red_lgC	ECOD (1.6)
B	Ribonuc_red_lgN_1	e1xjnB3	A: alpha arrays	X: RuvA-C	H: ATP cone (From Topology)	T: ATP cone	F: Ribonuc_red_lgN_1	ECOD (1.6)
B	Ribonuc_red_lgC	e1xjnB1	A: a/b barrels	X: Ten stranded beta/alpha barrel (From Topology)	H: Ten stranded beta/alpha barrel (From Topology)	T: Ten stranded beta/alpha barrel	F: Ribonuc_red_lgC	ECOD (1.6)
C	Ribonuc_red_lgN_1	e1xjnC2	A: alpha arrays	X: RuvA-C	H: ATP cone (From Topology)	T: ATP cone	F: Ribonuc_red_lgN_1	ECOD (1.6)
C	Ribonuc_red_lgC	e1xjnC1	A: a/b barrels	X: Ten stranded beta/alpha barrel (From Topology)	H: Ten stranded beta/alpha barrel (From Topology)	T: Ten stranded beta/alpha barrel	F: Ribonuc_red_lgC	ECOD (1.6)
D	Ribonuc_red_lgN_1	e1xjnD2	A: alpha arrays	X: RuvA-C	H: ATP cone (From Topology)	T: ATP cone	F: Ribonuc_red_lgN_1	ECOD (1.6)
D	Ribonuc_red_lgC	e1xjnD1	A: a/b barrels	X: Ten stranded beta/alpha barrel (From Topology)	H: Ten stranded beta/alpha barrel (From Topology)	T: Ten stranded beta/alpha barrel	F: Ribonuc_red_lgC	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.70.20	Alpha Beta	Alpha-Beta Barrel	Anaerobic Ribonucleotide-triphosphate Reductase Large Chain		CATH (4.3.0)
B	3.20.70.20	Alpha Beta	Alpha-Beta Barrel	Anaerobic Ribonucleotide-triphosphate Reductase Large Chain		CATH (4.3.0)
C	3.20.70.20	Alpha Beta	Alpha-Beta Barrel	Anaerobic Ribonucleotide-triphosphate Reductase Large Chain		CATH (4.3.0)
D	3.20.70.20	Alpha Beta	Alpha-Beta Barrel	Anaerobic Ribonucleotide-triphosphate Reductase Large Chain		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02867	Ribonucleotide reductase, barrel domain (Ribonuc_red_lgC)	Ribonucleotide reductase, barrel domain	-	Family
A, B, C, D	PF00317	Ribonucleotide reductase, all-alpha domain (Ribonuc_red_lgN)	Ribonucleotide reductase, all-alpha domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	ribonucleotide reductase, B12-dependent	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 vitamin binding cobalamin binding tetrapyrrole binding ribonucleoside-diphosphate reductase activity oxidoreductase activity oxidoreductase activity, acting on CH or CH2 groups oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor catalytic activity	cellular biosynthetic process cellular metabolic process primary metabolic process DNA metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process biosynthetic process metabolic process cellular process macromolecule metabolic process DNA biosynthetic process cellular biosynthetic process cellular metabolic process primary metabolic process DNA metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process biosynthetic process metabolic process cellular process macromolecule metabolic process DNA biosynthetic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process nucleotide biosynthetic process carbohydrate derivative metabolic process nucleotide metabolic process deoxyribonucleotide biosynthetic process deoxyribonucleotide metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process organophosphate biosynthetic process phosphate-containing compound metabolic process nucleoside phosphate biosynthetic process small molecule metabolic process phosphorus metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR008926	Ribonucleotide reductase R1 subunit, N-terminal	Homologous Superfamily
A, B, C, D	IPR013509	Ribonucleotide reductase large subunit, N-terminal	Domain
A, B, C, D	IPR013344	Ribonucleotide reductase, adenosylcobalamin-dependent	Family
A, B, C, D	IPR000788	Ribonucleotide reductase large subunit, C-terminal	Domain
A, B, C, D	IPR050862	Ribonucleoside diphosphate reductase class-2	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.