2e15

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='2e15' size='340' side='right'caption='[[2e15]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2e15' size='340' side='right'caption='[[2e15]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2e15]] 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=2E15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E15 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2e15]] 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=2E15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E15 FirstGlance]. <br>
-
</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>
+
</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>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wng|1wng]], [[2e16|2e16]], [[2e17|2e17]]</div></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>
-
<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=2e15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e15 OCA], [https://pdbe.org/2e15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e15 RCSB], [https://www.ebi.ac.uk/pdbsum/2e15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e15 ProSAT], [https://www.topsan.org/Proteins/RSGI/2e15 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=2e15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e15 OCA], [https://pdbe.org/2e15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e15 RCSB], [https://www.ebi.ac.uk/pdbsum/2e15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e15 ProSAT], [https://www.topsan.org/Proteins/RSGI/2e15 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 28: Line 27:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Diphthine synthase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Pyrococcus horikoshii]]
+
[[Category: Pyrococcus horikoshii OT3]]
-
[[Category: Kunishima, N]]
+
[[Category: Kunishima N]]
-
[[Category: Matsuura, Y]]
+
[[Category: Matsuura Y]]
-
[[Category: Mizutani, H]]
+
[[Category: Mizutani H]]
-
[[Category: Structural genomic]]
+
-
[[Category: National project on protein structural and functional analyse]]
+
-
[[Category: Nppsfa]]
+
-
[[Category: Rsgi]]
+
-
[[Category: Transferase]]
+

Revision as of 08:33, 25 October 2023

Crystal structure of Arg173 to Asn mutant of Diphthine synthase

PDB ID 2e15

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools