5a27: Difference between revisions

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-'''Unreleased structure'''
-The entry 5a27 is ON HOLD
+==Leishmania major N-myristoyltransferase in complex with a chlorophenyl 1,2,4-oxadiazole inhibitor.==
+<StructureSection load='5a27' size='340' side='right'caption='[[5a27]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5a27]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A27 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.37&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MYA:TETRADECANOYL-COA'>MYA</scene>, <scene name='pdbligand=TUT:5-CHLORANYL-N-[2-(3-METHOXYPHENYL)ETHANIMIDOYL]-2-PIPERIDIN-4-YLOXY-BENZAMIDE'>TUT</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5a27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a27 OCA], [https://pdbe.org/5a27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a27 RCSB], [https://www.ebi.ac.uk/pdbsum/5a27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a27 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q4Q5S8_LEIMA Q4Q5S8_LEIMA] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+N-Myristoyltransferase (NMT) is a potential drug target in Leishmania parasites. Scaffold-hopping from published inhibitors yielded the serendipitous discovery of a chemotype selective for Leishmania donovani NMT; development led to high affinity inhibitors with excellent ligand efficiency. The binding mode was characterised by crystallography and provides a structural rationale for selectivity.
-Authors: Rackham, M.D., Yu, Z., Brannigan, J.A., Heal, W.P., Paape, D., Barker, K.V., Wilkinson, A.J., Smith, D.F., Tate, E.W., Leatherbarrow, R.J.
+Discovery of high affinity inhibitors of -myristoyltransferase.,Rackham MD, Yu Z, Brannigan JA, Heal WP, Paape D, Barker KV, Wilkinson AJ, Smith DF, Leatherbarrow RJ, Tate EW Medchemcomm. 2015 Oct 8;6(10):1761-1766. Epub 2015 Aug 19. PMID:26962429<ref>PMID:26962429</ref>
-Description: Leishmania major N-myristoyltransferase in complex with a chlorophenyl inhibitor (compound 10j).
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Paape, D]]
+<div class="pdbe-citations 5a27" style="background-color:#fffaf0;"></div>
-[[Category: Yu, Z]]
+== References ==
-[[Category: Wilkinson, A.J]]
+<references/>
-[[Category: Leatherbarrow, R.J]]
+__TOC__
-[[Category: Brannigan, J.A]]
+</StructureSection>
-[[Category: Rackham, M.D]]
+[[Category: Large Structures]]
-[[Category: Heal, W.P]]
+[[Category: Leishmania major]]
-[[Category: Tate, E.W]]
+[[Category: Barker KV]]
-[[Category: Barker, K.V]]
+[[Category: Brannigan JA]]
-[[Category: Smith, D.F]]
+[[Category: Heal WP]]
+[[Category: Leatherbarrow RJ]]
+[[Category: Paape D]]
+[[Category: Rackham MD]]
+[[Category: Smith DF]]
+[[Category: Tate EW]]
+[[Category: Wilkinson AJ]]
+[[Category: Yu Z]]