5lym

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[[Image:5lym.gif|left|200px]]
 
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==STUDIES OF MONOCLINIC HEN EGG WHITE LYSOZYME. IV. X-RAY REFINEMENT AT 1.8 ANGSTROM RESOLUTION AND A COMPARISON OF THE VARIABLE REGIONS IN THE POLYMORPHIC FORMS==
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The line below this paragraph, containing "STRUCTURE_5lym", creates the "Structure Box" on the page.
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<StructureSection load='5lym' size='340' side='right'caption='[[5lym]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[5lym]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1lym 1lym]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LYM FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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{{STRUCTURE_5lym| PDB=5lym | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lym OCA], [https://pdbe.org/5lym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lym RCSB], [https://www.ebi.ac.uk/pdbsum/5lym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lym ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ly/5lym_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=5lym ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Monoclinic crystals of hen egg-white lysozyme (E.C. 3.2.1.17, HEL) grown at low pH in the presence of NaNO(3) belong to space group P2(1) with unit-cell dimensions, a = 28.0, b = 62.5, c = 60.9 A and beta= 90.8 degrees with two molecules in the asymmetric unit. 1.8 A resolution intensity data, collected on a CAD-4 diffractometer, contained 17 524 reflections with F &gt; 3sigma (93% complete). Our earlier preliminary 1.8 A model was refitted and refined using X-PLOR to an R value of 0.189. The deviations in the model from ideal geometry are 0.013 A in bond lengths and 2.8 degrees in bond angles. The r.m.s. deviation in the backbone atoms between the two molecules is 0.42 A. A comparison of HEL in different polymorphic crystal forms reveals that the prominent structural variability among them resides in two exposed regions 45-50 and 65-73 which are also regions of lattice contacts.
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'''STUDIES OF MONOCLINIC HEN EGG WHITE LYSOZYME. IV. X-RAY REFINEMENT AT 1.8 ANGSTROM RESOLUTION AND A COMPARISON OF THE VARIABLE REGIONS IN THE POLYMORPHIC FORMS'''
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Studies of monoclinic hen egg-white lysozyme. IV. X-ray refinement at 1.8 A resolution and a comparison of the variable regions in the polymorphic forms.,Rao ST, Sundaralingam M Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):170-5. PMID:15299739<ref>PMID:15299739</ref>
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==Overview==
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Monoclinic crystals of hen egg-white lysozyme (E.C. 3.2.1.17, HEL) grown at low pH in the presence of NaNO(3) belong to space group P2(1) with unit-cell dimensions, a = 28.0, b = 62.5, c = 60.9 A and beta= 90.8 degrees with two molecules in the asymmetric unit. 1.8 A resolution intensity data, collected on a CAD-4 diffractometer, contained 17 524 reflections with F &gt; 3sigma (93% complete). Our earlier preliminary 1.8 A model was refitted and refined using X-PLOR to an R value of 0.189. The deviations in the model from ideal geometry are 0.013 A in bond lengths and 2.8 degrees in bond angles. The r.m.s. deviation in the backbone atoms between the two molecules is 0.42 A. A comparison of HEL in different polymorphic crystal forms reveals that the prominent structural variability among them resides in two exposed regions 45-50 and 65-73 which are also regions of lattice contacts.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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5LYM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1lym 1lym]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LYM OCA].
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</div>
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<div class="pdbe-citations 5lym" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Studies of monoclinic hen egg-white lysozyme. IV. X-ray refinement at 1.8 A resolution and a comparison of the variable regions in the polymorphic forms., Rao ST, Sundaralingam M, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):170-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299739 15299739]
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Lysozyme]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Rao ST]]
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[[Category: Rao, S T.]]
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[[Category: Sundaralingam M]]
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[[Category: Sundaralingam, M.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:35:46 2008''
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Current revision

STUDIES OF MONOCLINIC HEN EGG WHITE LYSOZYME. IV. X-RAY REFINEMENT AT 1.8 ANGSTROM RESOLUTION AND A COMPARISON OF THE VARIABLE REGIONS IN THE POLYMORPHIC FORMS

PDB ID 5lym

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