_EC 1.6.99.3 Nadh dehydrogenase. 10 PDB entries  
EC 1.-.-.- Oxidoreductases. [8,653 PDB entries]
EC 1.6.-.- Acting on Nadh or nadph. [237 PDB entries]
EC 1.6.99.- With other acceptors. [46 PDB entries]
EC 1.6.99.3 Nadh dehydrogenase. [10 PDB entries]    
1nox

Reaction: Nadh + acceptor = NAD(+) + reduced acceptor.
 


NADH
+ acceptor
=
NAD(+)
+ reduced acceptor
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Beta-Nadh dehydrogenase dinucleotide. Cytochrome c reductase. Diaphorase. Dihydrocodehydrogenase I dehydrogenase. Dihydronicotinamide adenine dinucleotide dehydrogenase. Diphosphopyrinase. Dpnh diaphorase. Nadh diaphorase. Nadh hydrogenase. Nadh oxidoreductase.
Cofactor(s): Flavoprotein; Iron-sulfur.
 
Flavoprotein

Iron-sulfur
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments: After preparations have been subjected to certain treatments cytochrome c may act as acceptor. Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. Present in a mitochondrial complex as Ec 1.6.5.3. Formerly Ec 1.6.2.1.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 10 PDB entries in enzyme class E.C.1.6.99.3

  PDB code Protein
1nox
Nadh oxidase from thermus thermophilus
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Atcc: 27634. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (200 residues) CATH domain: 3.40.109.10
Bound ligand:   Het Group FMN is 41.51% similar to enzyme reactant NADH
1ozk
Theoretical model for nadh-ubiquinone reductase
Source: Escherichia coli. Bacteria
Chain: A (385 residues)
Bound ligand:   Het Group NAD corresponds to enzyme reactant NADH
2bc0
Structural analysis of streptococcus pyogenes nadh oxidase: wild-type nox
Source: Streptococcus pyogenes. Organism_taxid: 1314. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (473 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
2bc1
Structural analysis of streptococcus pyogenes nadh oxidase: c44s nox
Source: Streptococcus pyogenes. Organism_taxid: 1314. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (473 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
2bcp
Structural analysis of streptococcus pyogenes nadh oxidase: c44s nox with azide
Source: Streptococcus pyogenes. Organism_taxid: 1314. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (473 residues) CATH domains: 3.50.50.60 3.50.50.60 3.30.390.30
3f8d
Structure of sulfolobus solfataricus thioredoxin reductase mutant c147a
Source: Sulfolobus solfataricus. Organism_taxid: 2287. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (308 residues) CATH domains: 3.50.50.60 3.50.50.60
Bound ligand:   Het Group FAD is 76.00% similar to enzyme reactant NADH
3f8p
Structure of sulfolobus solfataricus trxr-b3
Source: Sulfolobus solfataricus. Organism_taxid: 2287. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (307 residues) CATH domains: 3.50.50.60 3.50.50.60
Bound ligand:   Het Group NAD is 61.00% similar to enzyme reactant NADH
3f8r
Crystal structure of sulfolobus solfataricus thioredoxin reductase b3 in complex with two NADP molecules
Source: Sulfolobus solfataricus. Organism_taxid: 2287. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (308 residues) CATH domains: 3.50.50.60 3.50.50.60
Bound ligand:   Het Group NAP is 91.00% similar to enzyme reactant NADH
3h8i
The first x-ray structure of a sulfide:quinone oxidoreductase: insights into sulfide oxidation mechanism
Source: Acidianus ambivalens. Desulfurolobus ambivalens. Organism_taxid: 2283
Chains: A, B (356 residues) CATH domain: 3.50.50.60
Bound ligand:   Het Group FAD is 76.00% similar to enzyme reactant NADH
3h8l
The first x-ray structure of a sulfide:quinone oxidoreductase: insights into sulfide oxidation mechanism
Source: Acidianus ambivalens. Desulfurolobus ambivalens. Organism_taxid: 2283
Chains: A, B (356 residues) CATH domain: 3.50.50.60
Bound ligand:   Het Group FAD is 76.00% similar to enzyme reactant NADH