5lo1: Difference between revisions

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 ==HSP90 WITH indazole derivative==
-<StructureSection load='5lo1' size='340' side='right' caption='[[5lo1]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='5lo1' size='340' side='right'caption='[[5lo1]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5lo1]] is a 1 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=5LO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LO1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5lo1]] is a 1 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=5LO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LO1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=70L:1-[2-Amino-4-(1,3-dihydro-isoindole-2-carbonyl)-quinazolin-6-yl]-cyclobutanecarboxylic+acid+ethylamide'>70L</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]] 2.7&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4eeh|4eeh]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=70L:1-[2-Amino-4-(1,3-dihydro-isoindole-2-carbonyl)-quinazolin-6-yl]-cyclobutanecarboxylic+acid+ethylamide'>70L</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5lo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lo1 OCA], [https://pdbe.org/5lo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lo1 RCSB], [https://www.ebi.ac.uk/pdbsum/5lo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lo1 ProSAT]</span></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=5lo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lo1 OCA], [http://pdbe.org/5lo1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lo1 RCSB], [http://www.ebi.ac.uk/pdbsum/5lo1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lo1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>
+[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 19: @@
 </div>
 <div class="pdbe-citations 5lo1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Amaral, M]]
+[[Category: Large Structures]]
-[[Category: Graedler, U]]
+[[Category: Amaral M]]
-[[Category: Schuetz, D]]
+[[Category: Graedler U]]
-[[Category: Chaperone]]
+[[Category: Schuetz D]]