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Molecular Graphics Resource

Eric C. Niederhoffer, Ph.D.

Associate Professor of Biochemistry and Molecular Biology

Southern Illinois University School of Medicine
600 Agriculture Drive, Carbondale, IL 62901-6503
Rm 112 Lindegren, 618-453-6467
eniederhoffer@siumed.edu
Copyright 2000- , E.C. Niederhoffer.
All Rights Reserved. All trademarks and copyrights are the property of their respective owners.
Ferredoxin-NADP+ reductase uncomplexed (1gaw) and complexed with ferredoxin (1gaq) from Zea mays

Kurisu, G., Kusunoki, M., Katoh, E., Yamazaki, T., Teshima, K., Onda, Y., Kimata-Ariga, Y., Hase, T. 2001. Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP+ reductase Nat. Struct. Biol. 8:117-121.


Ferredoxin-Fd-NADP+ reductase (1gaw)

Ferredoxin-Fd-NADP+ reductase-Fd (1gaq)

Active Site View

  • Push the button  to observe the following residues surrounding the FAD:
Arg93, Cys114, Cys132, Glu312, Leu94, Lys116, Ser96, Ser133, Tyr95, Tyr314, Val115, Val313 and five water molecules
  • Push the button  to observe the following residues that will form a hydrophobic contact region:
Leu94, Val92, Val151, Val313
  • Push the button  to observe the following residues that will form salt bridges:
Arg305, Asp84, Glu154, Glu278, Glu312, Lys33, Lys35, Lys85, Lys88, Lys91, Lys153, Lys301, Lys304

Push button  for Original View

Active Site View

  • Push the button  to observe the following residues surrounding the FAD:
Arg93, Cys114, Cys132, Glu94, Glu312, Leu94, Lys116, Ser96, Ser133, Tyr95, Tyr314, Val115, Val313 and two water molecules
  • Push the button  to observe the following residues within 3.0 Å of the iron-sulfur cluster:
Cys39, Cys44, Cys47, Cys77
  • Push the button  to observe the following residues forming a hydrophobic contact region (Fd is yellow):
Ala41, Cys39, Cys44, Leu94, Tyr37, Tyr63, Val92, Val151, Val313
  • Push the button  to observe the following residues forming salt bridges (Fd is yellow):
Arg40, Arg305, Asp31, Asp34, Asp60, Asp66, Asp65, Asp84, Glu29, Glu30, Glu154, Glu278, Glu312, Lys33, Lys35, Lys85, Lys88, Lys91, Lys153, Lys301, Lys304

Push button  for Original View


 

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For more information or comments about this page contact:
eniederhoffer@siumed.edu