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5g21

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'''Unreleased structure'''
 
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The entry 5g21 is ON HOLD
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==Leishmania major N-myristoyltransferase in complex with a quinoline inhibitor (compound 26).==
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<StructureSection load='5g21' size='340' side='right'caption='[[5g21]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5g21]] 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=5G21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G21 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<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=YN4:ETHYL+4-[(2-CYANOETHYL)SULFANYL]-6-{[6-(PIPERAZIN-1-YL)'>YN4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5g21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g21 OCA], [https://pdbe.org/5g21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g21 RCSB], [https://www.ebi.ac.uk/pdbsum/5g21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g21 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falciparum N-myristoyltransferase (NMT).
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Authors: Goncalves, V., Brannigan, J.A., Laporte, A., Bell, A.S., Roberts, S.M., Wilkinson, A.J., Leatherbarrow, R.J., Tate, E.W.
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Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.,Goncalves V, Brannigan JA, Laporte A, Bell AS, Roberts SM, Wilkinson AJ, Leatherbarrow RJ, Tate EW Medchemcomm. 2017 Jan 1;8(1):191-197. doi: 10.1039/c6md00531d. Epub 2016 Nov 11. PMID:28626547<ref>PMID:28626547</ref>
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Description: Leishmania major N-myristoyltransferase in complex with a quinoline inhibitor (compound 26).
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Wilkinson, A.J]]
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<div class="pdbe-citations 5g21" style="background-color:#fffaf0;"></div>
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[[Category: Leatherbarrow, R.J]]
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== References ==
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[[Category: Brannigan, J.A]]
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<references/>
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[[Category: Goncalves, V]]
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__TOC__
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[[Category: Roberts, S.M]]
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</StructureSection>
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[[Category: Tate, E.W]]
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[[Category: Large Structures]]
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[[Category: Laporte, A]]
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[[Category: Leishmania major]]
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[[Category: Bell, A.S]]
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[[Category: Bell AS]]
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[[Category: Brannigan JA]]
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[[Category: Goncalves V]]
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[[Category: Laporte A]]
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[[Category: Leatherbarrow RJ]]
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[[Category: Roberts SM]]
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[[Category: Tate EW]]
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[[Category: Wilkinson AJ]]

Current revision

Leishmania major N-myristoyltransferase in complex with a quinoline inhibitor (compound 26).

PDB ID 5g21

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