1.18.1.1: rubredoxin-NAD+ reductase
This is an abbreviated version!
For detailed information about rubredoxin-NAD+ reductase, go to the full flat file.
Reaction
Synonyms
(flavo)rubredoxin reductase, ABO_0162, dihydronicotinamide adenine dinucleotide-rubredoxin reductase, DPNH-rubredoxin reductase, EC 1.6.7.2, FIRd-reductase, NAD(P)H:rubredoxin reductase, NADH-rubredoxin oxidoreductase, NADH-rubredoxin reductase, NADH: rubredoxin oxidoreductase, NADH:rubredoxin oxidoreductase, NOR, NROR, RdxR, reduced nicotinamide adenine dinucleotide-rubredoxin reductase, reductase, rubredoxin-nicotinamide adenine dinucleotide, rubB, rubredoxin reductase, rubredoxin-NAD reductase
ECTree
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Subunits
Subunits on EC 1.18.1.1 - rubredoxin-NAD+ reductase
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dimer
RdxR consists of two cofactor-binding domains and a C-terminal domain essential for the specific recognition of Rdx, crystal structure analysis, dimerization restricts access to the NAD(P)H binding pocket and results in a steric clash between the modeled adenine moiety of NAD(P)H and alpha-helix alpha8' of the neighboring molecule, RdxR dimers form at high protein concentrations used during crystallization, rather than being functionally relevant, overview
monomer
additional information
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enzyme interacts with its physiological partner NADH:flavorubredoxin oxidoreductase. Redox properties and mechanism of electron transfer are fine-tuned upon the interaction
monomer
NROR exists as a monomer in solution, the overall structure of NROR displays a GR-fold