2e8q: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
Line 3: Line 3:
<StructureSection load='2e8q' size='340' side='right'caption='[[2e8q]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='2e8q' size='340' side='right'caption='[[2e8q]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2e8q]] 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=2E8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E8Q FirstGlance]. <br>
<table><tr><td colspan='2'>[[2e8q]] 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=2E8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E8Q FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2e8r|2e8r]], [[2e8s|2e8s]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8q OCA], [https://pdbe.org/2e8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e8q RCSB], [https://www.ebi.ac.uk/pdbsum/2e8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e8q ProSAT], [https://www.topsan.org/Proteins/RSGI/2e8q 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=2e8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e8q OCA], [https://pdbe.org/2e8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e8q RCSB], [https://www.ebi.ac.uk/pdbsum/2e8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e8q ProSAT], [https://www.topsan.org/Proteins/RSGI/2e8q TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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>
[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]]
Line 25: Line 24:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Diphthine synthase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Asada, Y]]
[[Category: Asada Y]]
[[Category: Kunishima, N]]
[[Category: Kunishima N]]
[[Category: Nakamoto, T]]
[[Category: Nakamoto T]]
[[Category: Structural genomic]]
[[Category: Shimada H]]
[[Category: Shimada, H]]
[[Category: Taketa M]]
[[Category: Taketa, M]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Rsgi]]
[[Category: Transferase]]

Latest revision as of 18:48, 29 May 2024

Structural study of Project ID PH0725 from Pyrococcus horikoshii OT3 (K19M)

2e8q, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA