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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.
Zinc-containing alkaline phosphatase (1alk) from Escherichia coli and the iron-containing purple acid phosphatase (1qhw) from Rattus norvegicus

Kim, E. E., Wyckoff, H. W. 1991. Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis. J. Mol. Biol. 218:449-464.

Lindqvist, Y., E. Johansson, H. Kaija, P. Vihko, and G. Schneider. 1999. Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 Å resolution with a µ-(hydr)oxo bridged di-iron center J. Mol. Biol. 291:135-147.

Alkaline phosphatase (1alk)

Purple acid phosphatase (1qhw)

Active Site View

  • Push the button  to observe the following residues within 3.0 Å of the binuclear zinc and magnesium sites:
Asp51, Asp327, Asp369, Glu322, His331, His370, His412, Ser102, Thr155, one phosphate 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 binuclear iron and zinc sites:
Asp35, Asp73, Asn112, His207, His216, His242, His244, Tyr76, one sulfate and four water ligands

Push button  for Original View

 

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eniederhoffer@siumed.edu