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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.
Copper,zinc- (1eso), iron- (1isa), and manganese- (1vew) containing superoxide dismutases from Escherichia coli

Pesce, A., C. Capasso, A. Battistoni, S. Folcarelli, G. Rotilio, A. Desideri, and M. Bolognesi. 1997. Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography. J. Mol. Biol. 274:408-420.

Lah, M. S., M. M. Dixon, K. A. Pattridge, W. C. Stallings, J. A. Fee, and M. L. Ludwig. 1995. Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry 34:1646-1660.

Edwards, R. A., H. M. Baker, M. M. Whittaker, J. W. Whittaker, G. B. Jameson, and E. N. Baker. 1998. Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1 Å resolution. J. Biol. Inorg. Chem. 3:161-171.

Copper,zinc superoxide dismutase

(1eso)

Iron superoxide dismutase

(1isa)

Manganese superoxide dismutase

(1vew)

Active Site View

  • Push the button  to observe the following residues within 3.0 Å of the copper,zinc centers:
Asp81, His44, His46, His61, His69, His78, His118

Push button  for Original View

Active Site View

  • Push the button  to observe the following residues within 3.0 Å of the iron center:
Asp156, His26, His73, His160, 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 manganese center:
Asp167, His26, His81, His171, and one hydroxide ion

Push button  for Original View

 

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