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4is2

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<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=4is2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4is2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4is2 RCSB], [http://www.ebi.ac.uk/pdbsum/4is2 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=4is2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4is2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4is2 RCSB], [http://www.ebi.ac.uk/pdbsum/4is2 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/BAIA2_EUBSP BAIA2_EUBSP]] 7-alpha-dehydroxylation of cholic acid and chenodeoxycholate, yielding deoxycholic acid and lithocholic acid, respectively. Highest affinity with taurochenodeoxycholic acid.
==See Also==
==See Also==

Revision as of 15:32, 25 December 2014

Crystal structure of the apo form of a 3alpha-hydroxysteroid dehydrogenase (BaiA2) associated with secondary bile acid synthesis from Clostridium scindens VPI12708 at 1.90 A resolution

4is2, resolution 1.90Å

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