1wde: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1wde]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WDE FirstGlance]. <br>
<table><tr><td colspan='2'>[[1wde]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WDE FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</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><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diphthine_synthase Diphthine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.98 2.1.1.98] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diphthine_synthase Diphthine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.98 2.1.1.98] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wde OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wde RCSB], [http://www.ebi.ac.uk/pdbsum/1wde PDBsum], [http://www.topsan.org/Proteins/RSGI/1wde TOPSAN]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wde OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wde RCSB], [http://www.ebi.ac.uk/pdbsum/1wde PDBsum], [http://www.topsan.org/Proteins/RSGI/1wde TOPSAN]</span></td></tr>
<table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/DPHB_AERPE DPHB_AERPE]] 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 (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Aeropyrum pernix]]
[[Category: Aeropyrum pernix]]
[[Category: Diphthine synthase]]
[[Category: Diphthine synthase]]
[[Category: Kishishita, S.]]
[[Category: Kishishita, S]]
[[Category: Murayama, K.]]
[[Category: Murayama, K]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Structural genomic]]
[[Category: Shirouzu, M.]]
[[Category: Shirouzu, M]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S]]
[[Category: Conserved hypothetical protein]]
[[Category: Conserved hypothetical protein]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Transferase]]
[[Category: Transferase]]