5nug: Difference between revisions

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 ==Motor domains from human cytoplasmic dynein-1 in the phi-particle conformation==
-<StructureSection load='5nug' size='340' side='right' caption='[[5nug]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+<SX load='5nug' size='340' side='right' viewer='molstar' caption='[[5nug]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5nug]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NUG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5nug]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NUG FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</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=5nug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nug OCA], [http://pdbe.org/5nug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nug RCSB], [http://www.ebi.ac.uk/pdbsum/5nug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nug ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5nug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nug OCA], [https://pdbe.org/5nug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nug RCSB], [https://www.ebi.ac.uk/pdbsum/5nug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nug ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/DYHC1_HUMAN DYHC1_HUMAN]] Autosomal dominant childhood-onset proximal spinal muscular atrophy without contractures;Autosomal dominant non-syndromic intellectual disability;Autosomal dominant Charcot-Marie-Tooth disease type 2O. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/DYHC1_HUMAN DYHC1_HUMAN] Autosomal dominant childhood-onset proximal spinal muscular atrophy without contractures;Autosomal dominant non-syndromic intellectual disability;Autosomal dominant Charcot-Marie-Tooth disease type 2O. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/DYHC1_HUMAN DYHC1_HUMAN]] Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Plays a role in mitotic spindle assembly and metaphase plate congression (PubMed:27462074).<ref>PMID:27462074</ref>
+[https://www.uniprot.org/uniprot/DYHC1_HUMAN DYHC1_HUMAN] Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Plays a role in mitotic spindle assembly and metaphase plate congression (PubMed:27462074).<ref>PMID:27462074</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 21: @@
 </div>
 <div class="pdbe-citations 5nug" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Dynein 3D structures|Dynein 3D structures]]
 == References ==
 <references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Carter, A P]]
+[[Category: Homo sapiens]]
-[[Category: Foster, H E]]
+[[Category: Large Structures]]
-[[Category: Zhang, K]]
+[[Category: Carter AP]]
-[[Category: Aaa+]]
+[[Category: Foster HE]]
-[[Category: Dynein]]
+[[Category: Zhang K]]
-[[Category: Motor domain]]
-[[Category: Motor protein]]