1rqc

<table><tr><td colspan='2'>[[1rqc]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RQC FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rl4|1rl4]], [[1jym|1jym]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 PLAFA])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqc OCA], [http://pdbe.org/1rqc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rqc RCSB], [http://www.ebi.ac.uk/pdbsum/1rqc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqc ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

An altered version of peptide deformylase from Plasmodium falciparum (PfPDF), the organism that causes the most devastating form of malaria, has been cocrystallized with a synthesized inhibitor that has submicromolar affinity for its target protein. The structure is solved at 2.2 A resolution, an improvement over the 2.8 A resolution achieved during the structural determination of unliganded PfPDF. This represents the successful outcome of modifying the protein construct in order to overcome adverse crystal contacts and other problems encountered in the study of unliganded PfPDF. Two molecules of PfPDF are found in the asymmetric unit of the current structure. The active site of each monomer of PfPDF is occupied by a proteolyzed fragment of the tripeptide-like inhibitor. Unexpectedly, each PfPDF subunit is associated with two nearly complete molecules of the inhibitor, found at a protein-protein interface. This is the first structure of a eukaryotic PDF protein, a potential drug target, in complex with a ligand.

An improved crystal form of Plasmodium falciparum peptide deformylase.,Robien MA, Nguyen KT, Kumar A, Hirsh I, Turley S, Pei D, Hol WG Protein Sci. 2004 Apr;13(4):1155-63. Epub 2004 Mar 9. PMID:15010544<ref>PMID:15010544</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1rqc" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Plafa]]

[[Category: Hirsh, I]]

[[Category: Hol, W G]]

[[Category: Kumar, A]]

[[Category: Nguyen, K T]]

[[Category: Pei, D]]

[[Category: Robien, M A]]

[[Category: Turley, S]]

[[Category: Hydrolase]]