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1hsw

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|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hsw OCA], [http://www.ebi.ac.uk/pdbsum/1hsw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hsw RCSB]</span>
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:56 2008''

Revision as of 18:09, 30 March 2008


PDB ID 1hsw

Drag the structure with the mouse to rotate
, resolution 2.00Å
Activity: Lysozyme, with EC number 3.2.1.17
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE)


Overview

The structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant have been solved and refined at 1.9 and 2.0 A resolution, respectively. A comparison of the native structure with those of crystals grown at acidic pH does not show any systematic pH-dependent difference in the molecular geometry. The conformations, mutual orientation and interactions of the catalytic residues Glu35 and Asp52 also remain unchanged. However, comparison between the native and low-humidity forms in the orthorhombic form show that the changes in molecular geometry which accompany the water-mediated transformation to the low-humidity form are more pronounced in the C-terminal residues than in the other regions of the molecule. During the transformation from the native to the low-humidity form, the locations of only about half the water molecules in the hydration shell remain unchanged, but the hydration shell as a whole moves along with the protein molecule.

About this Structure

1HSW is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant., Sukumar N, Biswal BK, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):934-7. PMID:10089340

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