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4add

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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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [http://www.ebi.ac.uk/pdbsum/4add 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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [http://www.ebi.ac.uk/pdbsum/4add PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ASTC_ECOLI ASTC_ECOLI]] Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.<ref>PMID:9696779</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 15:03, 25 December 2014

Structural and functional study of succinyl-ornithine transaminase from E. coli

4add, resolution 2.45Å

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