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3q43
From Proteopedia
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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=3q43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q43 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q43 RCSB], [http://www.ebi.ac.uk/pdbsum/3q43 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=3q43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q43 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q43 RCSB], [http://www.ebi.ac.uk/pdbsum/3q43 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 12:33, 25 December 2014
X-ray crystal structure of PfA-M1 bound to bestatin derivative 15
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