Chime SquareTM Animations

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.
Aconitase in the inactive (5acn) form from Sus scrofa (pig) and active forms (1c96, 1c97) from Bos taurus (bovine)

Robbins, A. H., and C. D. Stout. 1989. Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal. Proc. Natl. Acad. Sci. U.S.A. 86:3639-3643.

Lloyd, S. J., H. Lauble, G. S. Prasad, and C. D. Stout. 1999. The mechanism of aconitase: 1.8 Å crystal structure of the S642A: citrate complex. Protein Sci. 8:2655-2662.

Aconitase (5acn) inactive

Aconitase (1c96) active

Aconitase (1c97) active

Active Site View

  • Push the button  to observe the following residues within 3.0 Å of the iron-sulfur center:
Asn446, Cys358, Cys421, Cys424, and one water molecule

Push button  for Original View

Active Site View

  • Push the button  to observe the following residues within 3.0 Å of the iron-sulfur center and citrate:
Asp165, Arg447, Arg452, Arg580, Arg644, Cys358, Cys421, Cys424, Gln72, His101, His167, Ser166, Ser643, and one oxo ligand

Push button  for Original View

Active Site View

  • Push the button  to observe the following residues within 3.0 Å of the iron-sulfur center and isocitrate:
Asp165, Arg452, Arg580, Cys358, Cys421, Cys424, Gln72, His101, His167, Ser166, Ser643 and one oxo ligand

Push button  for Original View

 

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eniederhoffer@siumed.edu