6QTI

Structure of ovine transhydrogenase in the presence of NADP+ in a "double face-down" conformation

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD
Membrane Protein Annotation: mpstruc

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF02233	e6qtiA2	A: alpha bundles	X: Transhydrogeanse domain II (From Topology)	H: Transhydrogeanse domain II (From Topology)	T: Transhydrogeanse domain II	F: PF02233	ECOD (1.6)
A	PF12769	e6qtiA4	A: alpha bundles	X: Transhydrogeanse domain II (From Topology)	H: Transhydrogeanse domain II (From Topology)	T: Transhydrogeanse domain II	F: PF12769	ECOD (1.6)
A	PF01262	e6qtiA5	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF01262	ECOD (1.6)
A	PF02233	e6qtiA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PF02233	ECOD (1.6)
A	PF05222	e6qtiA3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: PF05222	ECOD (1.6)
B	PF02233	e6qtiB2	A: alpha bundles	X: Transhydrogeanse domain II (From Topology)	H: Transhydrogeanse domain II (From Topology)	T: Transhydrogeanse domain II	F: PF02233	ECOD (1.6)
B	PF12769	e6qtiB4	A: alpha bundles	X: Transhydrogeanse domain II (From Topology)	H: Transhydrogeanse domain II (From Topology)	T: Transhydrogeanse domain II	F: PF12769	ECOD (1.6)
B	PF01262	e6qtiB5	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF01262	ECOD (1.6)
B	PF02233	e6qtiB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PF02233	ECOD (1.6)
B	PF05222	e6qtiB3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: PF05222	ECOD (1.6)

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
A, B	PF02233	NAD(P) transhydrogenase beta subunit (PNTB)	NAD(P) transhydrogenase beta subunit	-	Family
A, B	PF12769	4TM region of pyridine nucleotide transhydrogenase, mitoch (PNTB_4TM)	4TM region of pyridine nucleotide transhydrogenase, mitoch	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Nicotinamide nucleotide transhydrogenase	oxidoreductase activity oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor NAD(P)+ transhydrogenase activity oxidoreductase activity, acting on NAD(P)H catalytic activity identical protein binding protein binding binding	transport proton transmembrane transport monoatomic ion transmembrane transport inorganic ion transmembrane transport establishment of localization inorganic cation transmembrane transport transmembrane transport monoatomic cation transmembrane transport localization monoatomic ion transport cellular process monoatomic cation transport	membrane-bounded organelle mitochondrial membrane intracellular anatomical structure organelle inner membrane mitochondrion membrane cellular anatomical entity intracellular membrane-bounded organelle mitochondrial inner membrane intracellular organelle organelle envelope mitochondrial envelope organelle cytoplasm membrane-bounded organelle mitochondrial membrane intracellular anatomical structure organelle inner membrane mitochondrion membrane cellular anatomical entity intracellular membrane-bounded organelle mitochondrial inner membrane intracellular organelle organelle envelope mitochondrial envelope organelle cytoplasm organelle membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR026255	NAD(P) transhydrogenase, alpha subunit	Family
A, B	IPR034300	NADP transhydrogenase beta-like domain	Domain
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	IPR024605	NAD(P) transhydrogenase, alpha subunit, C-terminal	Domain
A, B	IPR008143	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, conserved site-2	Conserved Site
A, B	IPR029035	DHS-like NAD/FAD-binding domain superfamily	Homologous Superfamily
A, B	IPR007698	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, NAD(H)-binding domain	Domain

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B	OPM	Transmembrane	Alpha-helical polytopic	Proton-translocating transhydrogenase	NAD(P) transhydrogenase

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A, B	MemProtMD	Annotated as membrane protein by MemProtMD

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A, B	mpstruc	TRANSMEMBRANE PROTEINS: ALPHA-HELICAL	Transhydrogenases	Nicotinamide nucleotide transhydrogenase (TH) proton channel, double face-down conformation

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 R01GM133198.