1bhz

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[[Image:1bhz.png|left|200px]]
 
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{{STRUCTURE_1bhz| PDB=1bhz | SCENE= }}
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==LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF HEN EGG WHITE LYSOZYME FROM MASC DATA==
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<StructureSection load='1bhz' size='340' side='right'caption='[[1bhz]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bhz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BHZ FirstGlance]. <br>
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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]] 3.9&#8491;</td></tr>
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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=1bhz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bhz OCA], [https://pdbe.org/1bhz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bhz RCSB], [https://www.ebi.ac.uk/pdbsum/1bhz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bhz 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/bh/1bhz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1bhz 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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A previous article [Fourme et al. (1995). J. Synchrotron Rad. 2, 36-48] presented the theoretical foundations of MASC, a new contrast-variation method using multiwavelength anomalous scattering, and reported the first experimental results. New experiments have been conducted both at the ESRF (Grenoble, France) and at LURE-DCI (Orsay, France), using cryocooled crystals of three proteins of known structures and very different molecular weights. Amplitudes of {GammaT(h)}, the 'normal' structure factors of the anomalously scattering part of the crystal including the solvent zone and the ordered anomalous scattering sites (if any), have been extracted from multiwavelength data. In the very low resolution range (d &gt;/= 20 A), the agreement between experimental {GammaT(h)} and model values calculated from the bulk solvent is all the more satisfactory since the molecular weight of the protein is high. For spacings between 10 and 20 A, the agreement between experimental {GammaT(h)} and model values is also satisfactory if one takes into account ordered anomalous scatterer sites. Such sites have been found in the three cases.
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===LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF HEN EGG WHITE LYSOZYME FROM MASC DATA===
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Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values.,Ramin M, Shepard W, Fourme R, Kahn R Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):157-67. Epub 1999, Jan 1. PMID:10089406<ref>PMID:10089406</ref>
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{{ABSTRACT_PUBMED_10089406}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 1bhz" style="background-color:#fffaf0;"></div>
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[[1bhz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHZ OCA].
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==See Also==
==See Also==
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*[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]]
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:010089406</ref><ref group="xtra">PMID:011679726</ref><references group="xtra"/>
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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: Fourme, R.]]
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[[Category: Fourme R]]
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[[Category: Kahn, R.]]
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[[Category: Kahn R]]
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[[Category: Ramin, M.]]
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[[Category: Ramin M]]
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[[Category: Shepard, W.]]
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[[Category: Shepard W]]
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[[Category: Hydrolase]]
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[[Category: Masc]]
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[[Category: Multiwavelength anomalous solvent contrast]]
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[[Category: O-glycosyl]]
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Current revision

LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF HEN EGG WHITE LYSOZYME FROM MASC DATA

PDB ID 1bhz

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