1.8.7.2	?	x * 13000, similar subunit, + x * 10000, variable subunit	706365	
1.8.7.2	?	x * ? + x * 10939, variable subunit, without known catalytic function, calculated	703528	
1.8.7.2	?	x * ? + x * 12669, subunit A, without a known catalytic function, calculated	703525	
1.8.7.2	?	x * ? + x * 12900, catalytic subunit, SDS-PAGE	702396	
1.8.7.2	?	x * ? + x * 12959, catalytic subunit, calculated	703527	
1.8.7.2	dimer	alpha/beta, peptide mapping for localization of labeled cysteinyl residues, overview	703527	
1.8.7.2	heterodimer	-	743317, 743549	
1.8.7.2	heterodimer	1 * 16000 + 1 * 14000, SDS-PAGE	743739	
1.8.7.2	homodimer	GvDTR is a homodimer with each monomer composed of two conserved Rossmann-type modules that form the FAD-binding and redox-active disulfide domains	-, 765599	
1.8.7.2	homodimer	x-ray crystallography	741911	
1.8.7.2	additional information	amino acid sequence of subunit A	703525	
1.8.7.2	additional information	amino acid sequence of the catalytic subunit. Six of the eight cysteine residues are clustered as Cys-Pro-Cys and Cys-His-Cys groups. Cysl9 and Cys27 are free cysteines with no catalytic function, Cys54 and Cys84 constitute the redox-active disulfide bridge of the active site, and the remaining four, Cys52, Cys71, Cys73, and Cys82 bind the Fe-S cluster	703527	
1.8.7.2	additional information	amino acid sequence of the variable subunit, without known catalytic function. the n-terminal consensus domain is possible involved in the interaction with the catalytic subunit	703528	
1.8.7.2	additional information	protein modulase is a complex protein composed of ferredoxin/thioredoxin reductase, ferredoxin, and thioredoxin. Buffer ionic strength affects the interactions among these proteins and in part determines the fate of the protein modulase complex in vitro. The ferredoxin and thioredoxin active in light modulation are not free in solution	706339