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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.
Iron-containing superoxide dismutase (1isa, 1isc) from Escherichia coli

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.

Iron superoxide dismutase (1isa)

Iron (azide) superoxide dismutase (1isc)

Active Site Views

  • Push the button  to observe the following residues within 3.0 Å of the iron center:
Asp156, His26, His73, His160, and one water (hydroxide) ligand
  • Push the button  to observe an extended hydrogen-bonding network about the iron center
  • Push the button  to observe an active-site channel for superoxide anion:
chain b is colored green
  • Push the button  to observe the following residues forming a hydrophobic interface between the subunits:
Ala141, Gly119, Ile164, Phe118, Trp158
  • Push the button  to observe the following residues forming a polar interface between the subunits:
Arg167, Asn65, Asn140, Asn168, Glu21, Glu159, Gln69, His30, His160, Lys29, Ser120, Ser139, Tyr25, Tyr34, Tyr163

Push button  for Original View

Active Site Views

  • Push the button  to observe the following residues within 3.0 Å of the iron center:
Asp156, His26, His73, His160, and one azide and water (hydroxide) ligands
  • Push the button  to observe an extended hydrogen-bonding network about the iron center
  • Push the button  to observe an active-site channel for superoxide anion:
chain b is colored green
  • Push the button  to observe the following residues forming a hydrophobic interface between the subunits:
Ala141, Gly119, Ile164, Phe118, Trp158
  • Push the button  to observe the following residues forming a polar interface between the subunits:
Arg167, Asn65, Asn140, Asn168, Glu21, Glu159, Gln69, His30, His160, Lys29, Ser120, Ser139, Tyr25, Tyr34, Tyr163

Push button  for Original View

 

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