1.8.5.8: eukaryotic sulfide quinone oxidoreductase
This is an abbreviated version!
For detailed information about eukaryotic sulfide quinone oxidoreductase, go to the full flat file.
Reaction
Synonyms
glutathione:CoQ reductase, HMT2, ScSQR, SQOR, SQR, Sqrdl, sulfide : quinone oxidoreductase, sulfide quinone oxidoreductase, sulfide:quinone oxidoreductase
ECTree
1.8.5.8 eukaryotic sulfide quinone oxidoreductaseAdvanced search results
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Cofactor on EC 1.8.5.8 - eukaryotic sulfide quinone oxidoreductase
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
additional information
molecular dynamics simulations and QM/MM reactivity predictors for a disulfide versus trisulfide cofactor involving FAD, overview
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FAD
required, FAD is noncovalently bound in an extended conformation and is in the oxidized state. The first Rossmann fold starts near the N-terminus and binds the ADP portion of FAD. The second Rossmann fold is closer to the isoalloxazine ring of FAD but is mostly positioned at least 10 A away from the flavin ring with one notable exception. FAD is bound in an extended conformation. Its interactions with the protein include 12 hydrogen bonds and electrostatic interactions with two helix dipoles. Two basic residues, Lys207 and Lys418, lie above the flavin's re- and si-face, respectively with their respective epsilon-amino groups 3.2 and 3.3 A from a carbonyl oxygen in the isoalloxazine ring (O4). Binding site structure, overview
FAD
the deduced ScSQR protein contains conserved FAD-binding domains, comprising residues 32-59, 121-134, and 306-331
