1dla

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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=1dla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dla OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dla RCSB], [http://www.ebi.ac.uk/pdbsum/1dla 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=1dla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dla OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dla RCSB], [http://www.ebi.ac.uk/pdbsum/1dla PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/ALDR_PIG ALDR_PIG]] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 08:55, 24 December 2014

NOVEL NADPH-BINDING DOMAIN REVEALED BY THE CRYSTAL STRUCTURE OF ALDOSE REDUCTASE

1dla, resolution 3.00Å

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