1.11.1.1	FAD	-	395331, 395332, 395333, 395338, 395344, 395345, 742429	
1.11.1.1	FAD	2 mol flavin and 1 mol of a non-flavin electron acceptor at the active site	395328	
1.11.1.1	FAD	enzyme contains flavin and non-flavin redox centers	395334, 395337, 395339, 395340	
1.11.1.1	FAD	FAD-flavoprotein, 1 mol FAD per 1 mol enzyme	395329	
1.11.1.1	FAD	flavoprotein. The resonance Raman (RR) modes of the oxidized and twoelectron reduced (EH2) forms of Npx are related to very tight flavin-protein interactions maintaining a nearly planar conformation of the isoalloxazine tricycle, a low level of H-bonding at the N1/N5 and O2/O4 sites, and a strong H-bond at N3H. Minimal changes in FAD structure and environment upon either NAD(H) binding or reduction of the sulfinic redox center	744823	
1.11.1.1	rubredoxin	rubredoxin-like Fe(SCys)4-domain	700055