The chitosanase from Streptomyces sp. N174
The 3D structure

Structural studies on the chitosanase from Streptomyces sp. N174 were done by the group of Dr. Jon D. Robertus (University of Texas at Austin) (38). Complete structural data are available from the Protein Data Bank (file 1CHK).

Click on the image on the right to see a rotating 3D model of the molecule.

The two amino acids represented in "ball and stick" format are the two catalytic residues GLU22 and ASP40.

The secondary structure elements in the chitosanase are arranged as follows: residues 7-23, a-helix; 28-33, a-helix; 34-36, b-strand; 42-47, b-strand; 50-54, b-strand; 56-69, a-helix; 74-85, a-helix; 94-107, a-helix; 107-125, a-helix; 125-134, a-helix; 136-150, a-helix; 158-170, a-helix; 178-197, a-helix; 203-217, a-helix; 225-229, b-strand; 232-236, b-strand.

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This page was created by Ryszard Brzezinski and Andrzej Neugebauer.
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Last updated: 1999/02/06