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4r3w

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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=4r3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r3w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r3w RCSB], [http://www.ebi.ac.uk/pdbsum/4r3w 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=4r3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r3w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r3w RCSB], [http://www.ebi.ac.uk/pdbsum/4r3w PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/A5MTN0_STREE A5MTN0_STREE]] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate (By similarity).[HAMAP-Rule:MF_02121]
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</StructureSection>
</StructureSection>

Revision as of 19:10, 25 December 2014

Crystal Structure Analysis of the 1,2,3-tricarboxylate benzoic acid bound to sp-ASADH-2'5'-ADP complex

4r3w, resolution 1.91Å

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