5aox: Difference between revisions

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 ==Human Alu RNA retrotransposition complex in the ribosome-stalling conformation==
-<StructureSection load='5aox' size='340' side='right' caption='[[5aox]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
+<StructureSection load='5aox' size='340' side='right'caption='[[5aox]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5aox]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AOX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AOX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5aox]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AOX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.04&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5aox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aox OCA], [http://pdbe.org/5aox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aox RCSB], [http://www.ebi.ac.uk/pdbsum/5aox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aox ProSAT]</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=5aox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aox OCA], [https://pdbe.org/5aox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aox RCSB], [https://www.ebi.ac.uk/pdbsum/5aox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aox ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SRP09_HUMAN SRP09_HUMAN]] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding. [[http://www.uniprot.org/uniprot/SRP14_HUMAN SRP14_HUMAN]] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.
+[https://www.uniprot.org/uniprot/SRP14_HUMAN SRP14_HUMAN] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5aox" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Signal recognition particle 3D structures|Signal recognition particle 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Ahl, V]]
+[[Category: Large Structures]]
-[[Category: Weichenrieder, O]]
+[[Category: Synthetic construct]]
-[[Category: Line]]
+[[Category: Ahl V]]
-[[Category: Mobile dna]]
+[[Category: Weichenrieder O]]
-[[Category: Protein targeting]]
-[[Category: Retrotransposition]]
-[[Category: Ribonucleoprotein particle]]
-[[Category: Rna]]
-[[Category: Signal recognition particle]]
-[[Category: Sine]]
-[[Category: Translation]]