1.6.2.2	FAD	-	392811, 394194, 394222, 394225, 657648, 657949, 658252, 658832, 659107, 659255, 659784, 685672, 696154, 696575, 699061, 711543, 712469, 712873, 713204, 741542, 741995, 742304, 742312, 742321, 742875, 743151, 743832	
1.6.2.2	FAD	1 mol FAD per mol enzyme	394203, 394218	
1.6.2.2	FAD	1 mol FAD per mol of recombinant enzyme	394199	
1.6.2.2	FAD	calculated results suggest that the electron and/or hydride ion transfer reaction from NADH to FAD can be accelerated in the presence of heme(Fe3+)	688620	
1.6.2.2	FAD	cytochrome b5 reductase is composed of one FAD and one NADH binding domain linked by a hinge region	685857	
1.6.2.2	FAD	flavoprotein, the FAD domain has a large cleft in which the FAD prosthetic group is located. The N-terminus of the NADH domain plays a hinge-connecting role between the two domains, the FAD and the NADH domains	724801	
1.6.2.2	FAD	non-covalentely bound prosthetic group	657675	
1.6.2.2	FAD	non-covalently bound in a large cleft between the two major domains	657460	
1.6.2.2	FAD	redox state of FAD during the b5R catalytic cycle and crystal structures comparion of the fully reduced form and the oxidized form, overview	725721	
1.6.2.2	FAD	the FAD cofactor is located in the cleft between the N-terminal FAD-binding domain and the C-terminal NADH-binding domain. The cofactor is located in the cleft between the two domains and interacts primarily with the FAD-binding domain	764860