2pb5

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Current revision (08:59, 25 October 2023) (edit) (undo)
 
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<StructureSection load='2pb5' size='340' side='right'caption='[[2pb5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='2pb5' size='340' side='right'caption='[[2pb5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2pb5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PB5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2pb5]] 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=2PB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PB5 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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 2.1&#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;'>[[2pb4|2pb4]]</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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=53953 'Pyrococcus shinkaii'])</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=2pb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pb5 OCA], [https://pdbe.org/2pb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pb5 RCSB], [https://www.ebi.ac.uk/pdbsum/2pb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pb5 ProSAT], [https://www.topsan.org/Proteins/RSGI/2pb5 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=2pb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pb5 OCA], [https://pdbe.org/2pb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pb5 RCSB], [https://www.ebi.ac.uk/pdbsum/2pb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pb5 ProSAT], [https://www.topsan.org/Proteins/RSGI/2pb5 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: Pyrococcus shinkaii]]
 
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[[Category: Diphthine synthase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kunishima, N]]
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[[Category: Pyrococcus horikoshii]]
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[[Category: Matsuura, Y]]
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[[Category: Kunishima N]]
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[[Category: Ono, N]]
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[[Category: Matsuura Y]]
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[[Category: Structural genomic]]
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[[Category: Ono N]]
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[[Category: Taketa, M]]
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[[Category: Taketa M]]
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[[Category: Yamamoto, H]]
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[[Category: Yamamoto H]]
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[[Category: Methyltransferase]]
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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: S-adenosyl-l-methionine]]
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[[Category: Transferase]]
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Current revision

Crystal structure of PH0725 from Pyrococcus horikoshii OT3

PDB ID 2pb5

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OCA

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