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4r5x

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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=4r5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r5x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r5x RCSB], [http://www.ebi.ac.uk/pdbsum/4r5x 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=4r5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r5x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r5x RCSB], [http://www.ebi.ac.uk/pdbsum/4r5x PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/AMP1_PLAFQ AMP1_PLAFQ]] Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC.<ref>PMID:12166515</ref> <ref>PMID:19196988</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 14:34, 25 December 2014

Structure of the m1 alanylaminopeptidase from malaria complexed with a hydroxamic acid-based inhibitor

4r5x, resolution 1.85Å

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