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.
1lzy
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1lzy.jpg|left|200px]] | + | [[Image:1lzy.jpg|left|200px]] |
| - | + | ||
| - | '''X-RAY STRUCTURE OF TURKEY EGG LYSOZYME COMPLEX WITH DI-N-ACETYLCHITOBIOSE. RECOGNITION AND BINDING OF ALPHA-ANOMERIC FORM''' | + | {{Structure |
| + | |PDB= 1lzy |SIZE=350|CAPTION= <scene name='initialview01'>1lzy</scene>, resolution 1.55Å | ||
| + | |SITE= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''X-RAY STRUCTURE OF TURKEY EGG LYSOZYME COMPLEX WITH DI-N-ACETYLCHITOBIOSE. RECOGNITION AND BINDING OF ALPHA-ANOMERIC FORM''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1LZY is a [ | + | 1LZY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LZY OCA]. |
==Reference== | ==Reference== | ||
| - | X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution., Harata K, Acta Crystallogr D Biol Crystallogr. 1993 Sep 1;49(Pt 5):497-504. PMID:[http:// | + | X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution., Harata K, Acta Crystallogr D Biol Crystallogr. 1993 Sep 1;49(Pt 5):497-504. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299509 15299509] |
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 16: | Line 25: | ||
[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:37:11 2008'' |
Revision as of 10:37, 20 March 2008
| |||||||
| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY STRUCTURE OF TURKEY EGG LYSOZYME COMPLEX WITH DI-N-ACETYLCHITOBIOSE. RECOGNITION AND BINDING OF ALPHA-ANOMERIC FORM
Overview
Monoclinic crystals of turkey egg lysozyme (TEL, E.C. 3.2.1.17) were obtained from 2.2 M ammonium sulfate solution at pH 4.2. They belong to space group P2(1) with unit-cell dimensions a = 38.07, b = 33.20, c = 46.12 A and beta = 110.1 degrees, and contain one molecule in the asymmetric unit (V(m) = 1.91 A(3) Da(-1)). The three-dimensional structure of TEL was solved by the method of multiple isomorphous replacement with anomalous scattering. Area detector data to 1.5 A resolution from native and heavy-atom derivatives were used for the structure determination. The structure was refined by the simulated-annealing method with diffraction data of 10-1.30 A resolution. The conventional R factor was 0.189. The root-mean-square deviations from ideal bond distances and angles were 0.016 A and 2.9 degrees, respectively. The backbone structure of TEL is very similar to that of hen egg lysozyme (HEL) and the difference in seven amino-acid residues does not affect the basic folding of the polypeptide chain. Except for the region from Gly101 to Gly104, the geometry of the active-site cleft is conserved between TEL and HEL. The Gly101 residue is located at the end of the sugar-binding site and the structural change in this region between TEL and HEL is considered to be responsible for the difference in their enzymatic properties.
About this Structure
1LZY is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution., Harata K, Acta Crystallogr D Biol Crystallogr. 1993 Sep 1;49(Pt 5):497-504. PMID:15299509
Page seeded by OCA on Thu Mar 20 12:37:11 2008
