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2b83
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2b83]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B83 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2b83]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B83 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jqb|1jqb]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jqb|1jqb]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b83 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2b83 RCSB], [http://www.ebi.ac.uk/pdbsum/2b83 PDBsum], [http://www.topsan.org/Proteins/ISPC/2b83 TOPSAN]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b83 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2b83 RCSB], [http://www.ebi.ac.uk/pdbsum/2b83 PDBsum], [http://www.topsan.org/Proteins/ISPC/2b83 TOPSAN]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ADH_CLOBE ADH_CLOBE]] 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 active with acetaldehyde and propionaldehyde.<ref>PMID:8349550</ref> <ref>PMID:20102159</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Clostridium beijerinckii]] | [[Category: Clostridium beijerinckii]] | ||
| - | [[Category: Dym, O | + | [[Category: Dym, O]] |
| - | [[Category: Goihberg, E | + | [[Category: Goihberg, E]] |
| - | [[Category: ISPC, Israel Structural Proteomics Center | + | [[Category: ISPC, Israel Structural Proteomics Center]] |
[[Category: Cbadh mutant]] | [[Category: Cbadh mutant]] | ||
| - | [[Category: ISPC]] | ||
| - | [[Category: Israel Structural Proteomics Center]] | ||
[[Category: Metal binding]] | [[Category: Metal binding]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
Revision as of 10:51, 25 December 2014
A single amino acid substitution in the Clostridium beijerinckii alcohol dehydrogenase is critical for thermostabilization
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