3w6a: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3w6a]] 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=3W6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W6A FirstGlance]. <br>
<table><tr><td colspan='2'>[[3w6a]] 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=3W6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W6A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RBN:BENZENERUTHENIUM(II)+CHLORIDE'>RBN</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4j7v|4j7v]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RBN:BENZENERUTHENIUM(II)+CHLORIDE'>RBN</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</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=3w6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w6a OCA], [https://pdbe.org/3w6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w6a RCSB], [https://www.ebi.ac.uk/pdbsum/3w6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w6a ProSAT]</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=3w6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w6a OCA], [https://pdbe.org/3w6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w6a RCSB], [https://www.ebi.ac.uk/pdbsum/3w6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w6a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[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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== Publication Abstract from PubMed ==
Porous protein crystals, which are protein assemblies in the solid state, have been engineered to form catalytic vessels by the incorporation of organometallic complexes. Ruthenium complexes in cross-linked porous hen egg white lysozyme (HEWL) crystals catalyzed the enantioselective hydrogen-transfer reduction of acetophenone derivatives. The crystals accelerated the catalytic reaction and gave different enantiomers based on the crystal form (tetragonal or orthorhombic). This method represents a new approach for the construction of bioinorganic catalysts from protein crystals.
 
Porous protein crystals as catalytic vessels for organometallic complexes.,Tabe H, Abe S, Hikage T, Kitagawa S, Ueno T Chem Asian J. 2014 May;9(5):1373-8. doi: 10.1002/asia.201301347. Epub 2014 Feb , 13. PMID:24677803<ref>PMID:24677803</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3w6a" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lysozyme]]
[[Category: Abe S]]
[[Category: Abe, S]]
[[Category: Hikage T]]
[[Category: Hikage, T]]
[[Category: Kitagawa S]]
[[Category: Kitagawa, S]]
[[Category: Tabe H]]
[[Category: Tabe, H]]
[[Category: Ueno T]]
[[Category: Ueno, T]]
[[Category: Hydrolase]]

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