2FRD

Structure of Transhydrogenase (dI.S138A.NADH)2(dIII.NADPH)1 asymmetric complex

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
B	d2frdb1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Formate/glycerate dehydrogenases, NAD-domain	Nicotinamide nucleotide transhydrogenase dI component	(Rhodospirillum rubrum ) [TaxId: 1085 ],	SCOPe (2.08)
B	d2frdb2	Alpha and beta proteins (a/b)	Flavodoxin-like	Formate/glycerate dehydrogenase catalytic domain-like	L-alanine dehydrogenase-like	Nicotinamide nucleotide transhydrogenase dI component	(Rhodospirillum rubrum ) [TaxId: 1085 ],	SCOPe (2.08)
A	d2frda1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Formate/glycerate dehydrogenases, NAD-domain	Nicotinamide nucleotide transhydrogenase dI component	(Rhodospirillum rubrum ) [TaxId: 1085 ],	SCOPe (2.08)
A	d2frda2	Alpha and beta proteins (a/b)	Flavodoxin-like	Formate/glycerate dehydrogenase catalytic domain-like	L-alanine dehydrogenase-like	Nicotinamide nucleotide transhydrogenase dI component	(Rhodospirillum rubrum ) [TaxId: 1085 ],	SCOPe (2.08)
C	d2frdc1	Alpha and beta proteins (a/b)	DHS-like NAD/FAD-binding domain	DHS-like NAD/FAD-binding domain	Transhydrogenase domain III (dIII)	Transhydrogenase domain III (dIII)	(Rhodospirillum rubrum ) [TaxId: 1085 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	D-2-hydroxyacid dehydrogenase-like	8057721	3000044	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	D-2-hydroxyacid dehydrogenase-like	8057721	3000044	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)
B	AlaDh_PNT_C	e2frdB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: AlaDh_PNT_C	ECOD (1.6)
B	AlaDh_PNT_N	e2frdB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: AlaDh_PNT_N	ECOD (1.6)
A	AlaDh_PNT_C	e2frdA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: AlaDh_PNT_C	ECOD (1.6)
A	AlaDh_PNT_N	e2frdA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: AlaDh_PNT_N	ECOD (1.6)
C	PNTB_C	e2frdC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PNTB_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
C	3.40.50.1220	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	TPP-binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF05222	Alanine dehydrogenase/PNT, N-terminal domain (AlaDh_PNT_N)	Alanine dehydrogenase/PNT, N-terminal domain	This family now also contains the lysine 2-oxoglutarate reductases.	Domain
A, B	PF01262	Alanine dehydrogenase/PNT, C-terminal domain (AlaDh_PNT_C)	Alanine dehydrogenase/PNT, C-terminal domain	This family now also contains the lysine 2-oxoglutarate reductases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	NAD(P) transhydrogenase subunit alpha part 1	NAD+ binding NAD binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding small molecule binding NADH binding oxidoreductase activity, acting on NAD(P)H as acceptor NAD+ binding NAD binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding small molecule binding NADH binding oxidoreductase activity, acting on NAD(P)H as acceptor oxidoreductase activity NAD(P)+ transhydrogenase (Si-specific) activity oxidoreductase activity, acting on NAD(P)H catalytic activity protein binding protein dimerization activity monoatomic cation transmembrane transporter activity proton transmembrane transporter activity primary active transmembrane transporter activity proton-translocating NAD(P)+ transhydrogenase activity active monoatomic ion transmembrane transporter activity oxidoreduction-driven active transmembrane transporter activity active transmembrane transporter activity inorganic molecular entity transmembrane transporter activity inorganic cation transmembrane transporter activity monoatomic ion transmembrane transporter activity transporter activity transmembrane transporter activity	nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process cellular metabolic process primary metabolic process generation of precursor metabolites and energy nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process nucleobase-containing compound metabolic process NADPH regeneration purine nucleotide metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process cellular metabolic process primary metabolic process generation of precursor metabolites and energy nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process nucleobase-containing compound metabolic process NADPH regeneration purine nucleotide metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process metabolic process cellular process small molecule metabolic process phosphorus metabolic process pyridine nucleotide metabolic process	-
C	NAD(P) transhydrogenase subunit beta	binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding monoatomic cation transmembrane transporter activity proton transmembrane transporter activity primary active transmembrane transporter activity proton-translocating NAD(P)+ transhydrogenase activity active monoatomic ion transmembrane transporter activity binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding monoatomic cation transmembrane transporter activity proton transmembrane transporter activity primary active transmembrane transporter activity proton-translocating NAD(P)+ transhydrogenase activity active monoatomic ion transmembrane transporter activity oxidoreduction-driven active transmembrane transporter activity active transmembrane transporter activity inorganic molecular entity transmembrane transporter activity inorganic cation transmembrane transporter activity monoatomic ion transmembrane transporter activity transporter activity transmembrane transporter activity	nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process cellular metabolic process primary metabolic process generation of precursor metabolites and energy nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process nucleobase-containing compound metabolic process NADPH regeneration purine nucleotide metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process cellular metabolic process primary metabolic process generation of precursor metabolites and energy nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process nucleobase-containing compound metabolic process NADPH regeneration purine nucleotide metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process metabolic process cellular process small molecule metabolic process phosphorus metabolic process pyridine nucleotide metabolic process	cell periphery plasma membrane membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR007886	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, N-terminal	Domain
A, B	IPR008142	Alanine dehydrogenase/NAD(P) transhydrogenase, conserved site-1	Conserved Site
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR008143	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, conserved site-2	Conserved Site
A, B	IPR007698	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, NAD(H)-binding domain	Domain
C	IPR034300	NADP transhydrogenase beta-like domain	Domain
C	IPR029035	DHS-like NAD/FAD-binding domain superfamily	Homologous Superfamily
C	IPR012136	NADP transhydrogenase, beta subunit	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.