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2lzt
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:2lzt.png|left|200px]] | ||
| - | < | + | ==REFINEMENT OF TRICLINIC LYSOZYME. II. THE METHOD OF STEREOCHEMICALLY RESTRAINED LEAST-SQUARES== |
| - | + | <StructureSection load='2lzt' size='340' side='right'caption='[[2lzt]], [[Resolution|resolution]] 1.97Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2lzt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LZT FirstGlance]. <br> | |
| - | + | </td></tr><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> | |
| - | -- | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lzt OCA], [https://pdbe.org/2lzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lzt RCSB], [https://www.ebi.ac.uk/pdbsum/2lzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lzt ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [[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> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lz/2lzt_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2lzt ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Refinement of triclinic lysozyme by restrained least squares against the 2 A resolution X-ray data is described, beginning with the model from cycle 17 of the preceding paper [Hodsdon, Brown, Sieker & Jensen (1990). Acta Cryst. B46, 54-62]. After 20 refinement cycles, R stood at 0.172. Nevertheless, serious errors involving both main-chain and side-chain atoms still remained, requiring numerous model rebuilding sessions interleaved with refinement cycles. After 63 cycles R = 0.124 for the model which includes all protein atoms, 249 water oxygen sites and five nitrate ions. Although the overall B is relatively low, 10.5 A2, B's for atoms in the region of residues 101-103, toward the termini of some of the longer side chains, and in the region of the C terminus of the main chain exceed 20 A2, indicating relatively high atomic mobilities, disorder, or remaining errors in the model. | ||
| - | + | Refinement of triclinic lysozyme: II. The method of stereochemically restrained least squares.,Ramanadham M, Sieker LC, Jensen LH Acta Crystallogr B. 1990 Feb 1;46 ( Pt 1):63-9. PMID:2302327<ref>PMID:2302327</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2lzt" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Chick]] |
| - | + | [[Category: Large Structures]] | |
| - | + | ||
| - | == | + | |
| - | < | + | |
| - | [[Category: | + | |
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
| - | [[Category: Jensen, L H | + | [[Category: Jensen, L H]] |
| - | [[Category: Ramanadham, M | + | [[Category: Ramanadham, M]] |
| - | [[Category: Sieker, L C | + | [[Category: Sieker, L C]] |
| - | + | ||
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Current revision
REFINEMENT OF TRICLINIC LYSOZYME. II. THE METHOD OF STEREOCHEMICALLY RESTRAINED LEAST-SQUARES
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