7uut: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7uut]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoanaerobacter_pseudethanolicus Thermoanaerobacter pseudethanolicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=7jnu 7jnu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UUT FirstGlance]. <br>
<table><tr><td colspan='2'>[[7uut]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoanaerobacter_pseudethanolicus Thermoanaerobacter pseudethanolicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=7jnu 7jnu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UUT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2RP:(2R)-pentan-2-ol'>2RP</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.89&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2RP:(2R)-pentan-2-ol'>2RP</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=7uut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uut OCA], [https://pdbe.org/7uut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uut RCSB], [https://www.ebi.ac.uk/pdbsum/7uut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uut 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=7uut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uut OCA], [https://pdbe.org/7uut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uut RCSB], [https://www.ebi.ac.uk/pdbsum/7uut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uut ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ADH_THEBR ADH_THEBR]] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.
[https://www.uniprot.org/uniprot/ADH_THEBR ADH_THEBR] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.


==See Also==
==See Also==

Latest revision as of 17:20, 18 October 2023

Ternary complex crystal structure of secondary alcohol dehydrogenases from the Thermoanaerobacter ethanolicus mutants C295A and I86A provides better understanding of catalytic mechanism

7uut, resolution 1.89Å

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