7rm6: Difference between revisions

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-'''Unreleased structure'''
-The entry 7rm6 is ON HOLD  until Paper Publication
+==Horse liver alcohol dehydrogenase in complex with NADH and N-cylcohexyl formamide==
+<StructureSection load='7rm6' size='340' side='right'caption='[[7rm6]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7rm6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RM6 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]] 1.43&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXF:CYCLOHEXYLFORMAMIDE'>CXF</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7rm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rm6 OCA], [https://pdbe.org/7rm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rm6 RCSB], [https://www.ebi.ac.uk/pdbsum/7rm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rm6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ADH1E_HORSE ADH1E_HORSE]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The catalytic power of an electric field depends on its magnitude and orientation with respect to the reactive chemical species. Understanding and designing new catalysts for electrostatic catalysis thus requires methods to measure the electric field orientation and magnitude at the molecular scale. We demonstrate that electric field orientations can be extracted using a two-directional vibrational probe by exploiting the vibrational Stark effect of both the C=O and C-D stretches of a deuterated aldehyde. Combining spectroscopy with molecular dynamics and electronic structure partitioning methods, we demonstrate that, despite distinct polarities, solvents act similarly in their preference for electrostatically stabilizing large bond dipoles at the expense of destabilizing small ones. In contrast, we find that for an active-site aldehyde inhibitor of liver alcohol dehydrogenase, the electric field orientation deviates markedly from that found in solvents, which provides direct evidence for the fundamental difference between the electrostatic environment of solvents and that of a preorganized enzyme active site.
-Authors:
+A two-directional vibrational probe reveals different electric field orientations in solution and an enzyme active site.,Zheng C, Mao Y, Kozuch J, Atsango AO, Ji Z, Markland TE, Boxer SG Nat Chem. 2022 Aug;14(8):891-897. doi: 10.1038/s41557-022-00937-w. Epub 2022 May , 5. PMID:35513508<ref>PMID:35513508</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7rm6" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Equus caballus]]
+[[Category: Large Structures]]
+[[Category: Boxer SG]]
+[[Category: Zheng C]]