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1fk8
From Proteopedia
(Difference between revisions)
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fjh|1fjh]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fjh|1fjh]]</td></tr> | ||
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-alpha- | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-alpha-hydroxysteroid_3-dehydrogenase_(Si-specific) 3-alpha-hydroxysteroid 3-dehydrogenase (Si-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.50 1.1.1.50] </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=1fk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fk8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fk8 PDBsum]</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=1fk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fk8 OCA], [http://pdbe.org/1fk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fk8 PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/DIDH_COMTE DIDH_COMTE]] Catalyzes the reversible interconversion of hydroxy and oxo groups at position 3 of the steroid nucleus. Along with the 3 alpha-hydroxysteroid dehydrogenase and 3-oxo-reductase activities towards a variety of cis or trans fused A/B ring steroids, it also reduces several xenobiotic carbonyl compounds, including a metyrapone-based class of insecticides, to the respective alcohol metabolites. No detectable activity on testosterone, progesterone or 3-oxo-desogestrel. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 1fk8" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Revision as of 05:41, 11 September 2015
THE CRYSTAL STRUCTURE OF THE BINARY COMPLEX WITH NAD OF 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE FROM COMAMONAS TESTOSTERONI, A MEMBER OF THE SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY
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Categories: Comamonas testosteroni | Ficner, R | Grimm, C | Klebe, G | Maser, E | Reuter, K | Carbonyl reductase | Hydroxysteroid | Metyrapone | Nad | Nicotinamide adenine dinucleotide | Oligomerisation | Oxidoreductase | Sdr | Short chain dehydrogenase | Steroid | Substrate binding loop | Xenobiotic
