PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12359874-2 2002 A conserved aromatic residue in the FNR module of NOS shields the isoalloxazine ring of FAD and is known to regulate NADPH binding affinity and specificity in related flavoproteins. isoalloxazine 66-79 ferredoxin reductase Homo sapiens 36-39 22542899-9 2012 The overall findings indicate that in FNR the volume of the residue at position 266 is essential to attain the catalytic architecture between the nicotinamide and isoalloxazine rings at the active site and, therefore, for an efficient HT process. isoalloxazine 163-176 ferredoxin reductase Homo sapiens 38-41 21538059-5 2012 In particular, the side chain of the C-terminal Y303 in Anabaena FNR appears key to providing the optimum geometry by reducing the stacking probability between the isoalloxazine and nicotinamide rings, thus providing the required co-linearity and distance among the N5 of the flavin cofactor, the C4 of the coenzyme nicotinamide and the hydride that has to be transferred between them. isoalloxazine 164-177 ferredoxin reductase Homo sapiens 65-68 20471952-7 2010 The architecture of the WT FNR active site precisely contributes to reduce the stacking probability between the isoalloxazine and nicotinamide rings in the catalytically competent complex, modulating the angle and distance between the N5 of the FAD isoalloxazine and the C4 of the coenzyme nicotinamide to values that ensure efficient HT processes. isoalloxazine 112-125 ferredoxin reductase Homo sapiens 27-30 11053423-8 2001 The [2Fe-2S] cluster of Adx and the isoalloxazine rings of FAD of AR are 10 A apart suggesting a possible electron transfer route between these redox centers. isoalloxazine 36-49 ferredoxin reductase Homo sapiens 66-68 11577105-1 2001 In ferredoxin-NADP(+) reductase (FNR), FAD is bound outside of an anti-parallel beta-barrel with the isoalloxazine lying in a two-tyrosine pocket. isoalloxazine 101-114 ferredoxin reductase Homo sapiens 3-31 11577105-1 2001 In ferredoxin-NADP(+) reductase (FNR), FAD is bound outside of an anti-parallel beta-barrel with the isoalloxazine lying in a two-tyrosine pocket. isoalloxazine 101-114 ferredoxin reductase Homo sapiens 33-36 7677850-1 1995 The crystal structure of ferredoxin-NADP+ reductase (FNR) suggests that Ser96 is directly involved in hydride transfer between the isoalloxazine moiety of FAD and the nicotinamide ring of NADP(H). isoalloxazine 131-144 ferredoxin reductase Homo sapiens 25-51 7626622-6 1995 The conserved sequence contains a tyrosine residue (Tyr-44) which, based on the X-ray crystal structure of ferredoxin-NADP+ reductase, is postulated to participate in FAD binding through van der Waals contact with the isoalloxazine ring and a hydrogen bond to the 3"-hydroxy of the ribityl moiety. isoalloxazine 218-231 ferredoxin reductase Homo sapiens 107-133 7677850-1 1995 The crystal structure of ferredoxin-NADP+ reductase (FNR) suggests that Ser96 is directly involved in hydride transfer between the isoalloxazine moiety of FAD and the nicotinamide ring of NADP(H). isoalloxazine 131-144 ferredoxin reductase Homo sapiens 53-56