2egl

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<StructureSection load='2egl' size='340' side='right'caption='[[2egl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2egl' size='340' side='right'caption='[[2egl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2egl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EGL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2egl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EGL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wng|1wng]]</div></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dphB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 Pyrococcus horikoshii])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Diphthine_synthase Diphthine synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.98 2.1.1.98] </span></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=2egl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2egl OCA], [https://pdbe.org/2egl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2egl RCSB], [https://www.ebi.ac.uk/pdbsum/2egl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2egl ProSAT], [https://www.topsan.org/Proteins/RSGI/2egl TOPSAN]</span></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=2egl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2egl OCA], [https://pdbe.org/2egl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2egl RCSB], [https://www.ebi.ac.uk/pdbsum/2egl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2egl ProSAT], [https://www.topsan.org/Proteins/RSGI/2egl TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DPHB_PYRHO DPHB_PYRHO]] S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.<ref>PMID:20873788</ref>
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[https://www.uniprot.org/uniprot/DPHB_PYRHO DPHB_PYRHO] S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.<ref>PMID:20873788</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Diphthine synthase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pyrococcus horikoshii]]
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[[Category: Pyrococcus horikoshii OT3]]
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[[Category: Kunishima, N]]
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[[Category: Krishna Swamy BS]]
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[[Category: Matsuura, Y]]
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[[Category: Kunishima N]]
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[[Category: Mizutani, H]]
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[[Category: Matsuura Y]]
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[[Category: Murthy, M R.N]]
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[[Category: Mizutani H]]
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[[Category: Structural genomic]]
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[[Category: Murthy MRN]]
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[[Category: Simanshu, D K]]
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[[Category: Simanshu DK]]
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[[Category: Swamy, B S.Krishna]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Rsgi]]
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[[Category: Transferase]]
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Revision as of 08:39, 25 October 2023

Crystal structure of Glu171 to Lys mutant of Diphthine synthase

PDB ID 2egl

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