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4r5m

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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=4r5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r5m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r5m RCSB], [http://www.ebi.ac.uk/pdbsum/4r5m 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=4r5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r5m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r5m RCSB], [http://www.ebi.ac.uk/pdbsum/4r5m PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/DHAS1_VIBCH DHAS1_VIBCH]] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.<ref>PMID:12071715</ref>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 12:15, 25 December 2014

Crystal structure of Vc-Aspartate beta-semialdehyde-dehydrogenase with NADP and 4-Nitro-2-Phosphono-Benzoic acid

4r5m, resolution 1.89Å

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