4j1b: Difference between revisions

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'''Unreleased structure'''


The entry 4j1b is ON HOLD
==X-ray structure of the adduct between hen egg white lysozyme and AziRu (black crystal)==
<StructureSection load='4j1b' size='340' side='right'caption='[[4j1b]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4j1b]] 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=4J1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J1B FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</scene></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=4j1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j1b OCA], [https://pdbe.org/4j1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j1b RCSB], [https://www.ebi.ac.uk/pdbsum/4j1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j1b 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>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The binding properties of AziRu, a ruthenium(III) complex with high antiproliferative activity, toward a hen egg white lysozyme have been investigated by X-ray crystallography and Raman microscopy. The data provide clear evidence on the mechanism of AziRu-protein adduct formation and of ligand exchange in the crystal state.


Authors: Vergara, A., Merlino, A
Interaction of Anticancer Ruthenium Compounds with Proteins: High-Resolution X-ray Structures and Raman Microscopy Studies of the Adduct between Hen Egg White Lysozyme and AziRu.,Vergara A, D'Errico G, Montesarchio D, Mangiapia G, Paduano L, Merlino A Inorg Chem. 2013 Mar 22. PMID:23517183<ref>PMID:23517183</ref>


Description: X-ray structure of the adduct between hen egg white lysozyme and AziRu (black crystal)
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4j1b" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Merlino A]]
[[Category: Vergara A]]

Latest revision as of 10:04, 27 November 2024

X-ray structure of the adduct between hen egg white lysozyme and AziRu (black crystal)X-ray structure of the adduct between hen egg white lysozyme and AziRu (black crystal)

Structural highlights

4j1b is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.66Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

Publication Abstract from PubMed

The binding properties of AziRu, a ruthenium(III) complex with high antiproliferative activity, toward a hen egg white lysozyme have been investigated by X-ray crystallography and Raman microscopy. The data provide clear evidence on the mechanism of AziRu-protein adduct formation and of ligand exchange in the crystal state.

Interaction of Anticancer Ruthenium Compounds with Proteins: High-Resolution X-ray Structures and Raman Microscopy Studies of the Adduct between Hen Egg White Lysozyme and AziRu.,Vergara A, D'Errico G, Montesarchio D, Mangiapia G, Paduano L, Merlino A Inorg Chem. 2013 Mar 22. PMID:23517183[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
  2. Vergara A, D'Errico G, Montesarchio D, Mangiapia G, Paduano L, Merlino A. Interaction of Anticancer Ruthenium Compounds with Proteins: High-Resolution X-ray Structures and Raman Microscopy Studies of the Adduct between Hen Egg White Lysozyme and AziRu. Inorg Chem. 2013 Mar 22. PMID:23517183 doi:http://dx.doi.org/10.1021/ic4004142

4j1b, resolution 1.66Å

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