This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1hsw
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
| |||||||
| , 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
Page seeded by OCA on Sun Mar 30 21:09:56 2008
