4z6k

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<StructureSection load='4z6k' size='340' side='right'caption='[[4z6k]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='4z6k' size='340' side='right'caption='[[4z6k]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4z6k]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Morse Morse]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z6K OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4Z6K FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4z6k]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Moraxella_sp._TAE123 Moraxella sp. TAE123]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z6K FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 1.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">adh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=191545 MORSE])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] </span></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=4z6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z6k OCA], [https://pdbe.org/4z6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z6k RCSB], [https://www.ebi.ac.uk/pdbsum/4z6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z6k ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4z6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z6k OCA], [http://pdbe.org/4z6k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z6k RCSB], [http://www.ebi.ac.uk/pdbsum/4z6k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z6k ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/ADH_MORSE ADH_MORSE] Psychrophilic alcohol dehydrogenase that exhibits a wide range of substrate specificity, oxidizing mainly primary and secondary aliphatic alcohols, utilizing NAD(+) as a cosubstrate. In vitro, shows highest reaction rates for ethanol as a substrate and gradually decreases its reaction rates as the length and branching of the carbon chain of the alcohol substrates increase. To a lesser extent, is also able to reduce aldehydes and ketones. Do not catalyze the further oxidation of aldehydes to carboxylic acids. Cannot use NADP(+) instead of NAD(+).<ref>PMID:9660191</ref>
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An NAD(+)-dependent psychrophilic alcohol dehydrogenase (ADH) from the Antarctic psychrophile Moraxella sp. TAE123 has been purified to homogeneity. The enzyme consists of four identical subunits, each containing two Zn ions. Protein crystals suitable for X-ray diffraction were obtained under optimized salting-out crystallization conditions using ammonium sulfate as a precipitating agent. The crystals are hexagonal bipyramids and belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = 136.4, c = 210.7 A. They contain one protein homotetramer in the asymmetric unit. Diffraction data were collected to 2.2 A under cryogenic conditions using synchrotron radiation.
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Crystallization and preliminary X-ray diffraction studies of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123.,Papanikolau Y, Tsigos I, Papadovasilaki M, Bouriotis V, Petratos K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Feb 1;61(Pt 2):246-8. Epub, 2005 Feb 1. PMID:16511007<ref>PMID:16511007</ref>
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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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<div class="pdbe-citations 4z6k" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alcohol dehydrogenase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Morse]]
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[[Category: Moraxella sp. TAE123]]
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[[Category: Bouriotis, V]]
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[[Category: Bouriotis V]]
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[[Category: Papanikolau, Y]]
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[[Category: Papanikolau Y]]
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[[Category: Petratos, K]]
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[[Category: Petratos K]]
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[[Category: Cold-adapted enzyme]]
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[[Category: Nad-dependent alcohol dehydrogenase]]
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[[Category: Oxidoreductase]]
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[[Category: Zinc-binding protein]]
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Current revision

Alcohol dehydrogenase from the antarctic psychrophile Moraxella sp. TAE 123

PDB ID 4z6k

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