Annotations: 5JWA

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	EUF07937	e5jwaA3	A: alpha arrays	X: EF-hand	H: Helical insertion domain in malaria PfNDH2 (From Topology)	T: Helical insertion domain in malaria PfNDH2	F: EUF07937	ECOD (1.6)
A	UNK_F_TYPE	e5jwaA4	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain (From Topology)	T: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain	F: UNK_F_TYPE	ECOD (1.6)
A	Pyr_redox_2	e5jwaA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Pyr_redox_2	ECOD (1.6)
B [auth H]	EUF07937	e5jwaH4	A: alpha arrays	X: EF-hand	H: Helical insertion domain in malaria PfNDH2 (From Topology)	T: Helical insertion domain in malaria PfNDH2	F: EUF07937	ECOD (1.6)
B [auth H]	UNK_F_TYPE	e5jwaH3	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain (From Topology)	T: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain	F: UNK_F_TYPE	ECOD (1.6)
B [auth H]	Pyr_redox_2	e5jwaH1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Pyr_redox_2	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth H]	PF22366	NDH2 C-terminal domain (NDH2_C)	NDH2 C-terminal domain	This entry represent the C-terminal domain of alternative NADH:quinone oxidoreductases known as NDH2 that deliver electrons to the respiratory chain by oxidation of NADH and reduction of quinones but does not pump protons. NDH-2 have particular relev ...	This entry represent the C-terminal domain of alternative NADH:quinone oxidoreductases known as NDH2 that deliver electrons to the respiratory chain by oxidation of NADH and reduction of quinones but does not pump protons. NDH-2 have particular relevance in yeasts like Saccharomyces cerevisiae and in several prokaryotes, whose respiratory chains are devoid of complex I, in which NDH-2 keep the balance and are the main entry point of electrons into the respiratory chains [2]. NDH2 proteins are found in bacteria, certain plant, fungal and protozoan mitochondria, but not in mammals, they have been used as a drug target for Mycoplasma tuberculosis, Plasmodium falciparum and Toxoplasma gondii [1,3].	Domain
A, B [auth H]	PF22365	PfNDH2 helical insertion domain (PfNDH2_hel_ins)	PfNDH2 helical insertion domain	This entry represent the helical insertion domain of NDH2, a NADH-ubiquinone oxidoreductase from Plasmodium falciparum [1], an interesting target for antimalarial drug development. This domain seems to be present exclusively in Plasmodium sequences.	Domain
A, B [auth H]	PF07992	Pyridine nucleotide-disulphide oxidoreductase (Pyr_redox_2)	Pyridine nucleotide-disulphide oxidoreductase	This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth H]	NADH dehydrogenase, putative	oxidoreductase activity NADPH:quinone reductase activity oxidoreductase activity, acting on NAD(P)H oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor catalytic activity NADH:ubiquinone reductase (non-electrogenic) activity NADH dehydrogenase activity binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding cation binding oxidoreductase activity NADPH:quinone reductase activity oxidoreductase activity, acting on NAD(P)H oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor catalytic activity NADH:ubiquinone reductase (non-electrogenic) activity NADH dehydrogenase activity binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding cation binding ion binding metal ion binding	nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process primary metabolic process nucleotide metabolic process NADH oxidation NAD metabolic process NADH metabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process primary metabolic process nucleotide metabolic process NADH oxidation NAD metabolic process NADH metabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process 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	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth H]	IPR023753	FAD/NAD(P)-binding domain	Domain
A, B [auth H]	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A, B [auth H]	IPR045024	Alternative NADH dehydrogenase	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.