This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2hux
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='2hux' size='340' side='right'caption='[[2hux]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2hux' size='340' side='right'caption='[[2hux]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2hux]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2hux]] 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=2HUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HUX FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=2hux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hux OCA], [https://pdbe.org/2hux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hux RCSB], [https://www.ebi.ac.uk/pdbsum/2hux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hux ProSAT], [https://www.topsan.org/Proteins/RSGI/2hux 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=2hux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hux OCA], [https://pdbe.org/2hux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hux RCSB], [https://www.ebi.ac.uk/pdbsum/2hux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hux ProSAT], [https://www.topsan.org/Proteins/RSGI/2hux 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> | |
== 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: Kunishima | + | [[Category: Kunishima N]] |
| - | + | [[Category: Sugahara M]] | |
| - | [[Category: Sugahara | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal structure of PH0725 from Pyrococcus horikoshii OT3
| |||||||||||
