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3q11

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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=3q11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q11 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q11 RCSB], [http://www.ebi.ac.uk/pdbsum/3q11 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=3q11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q11 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q11 RCSB], [http://www.ebi.ac.uk/pdbsum/3q11 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/A5MTN0_STRPN A5MTN0_STRPN]] 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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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 15:51, 25 December 2014

Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Streptococcus pneumoniae with NADP and aspartyl beta-difluorophosphonate

3q11, resolution 1.80Å

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