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3o2f

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==Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54==
==Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54==
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<StructureSection load='3o2f' size='340' side='right' caption='[[3o2f]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='3o2f' size='340' side='right'caption='[[3o2f]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3o2f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Canlf Canlf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O2F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3o2f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canlf Canlf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O2F FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=P54:8-[(2,4-DIMETHYLPHENYL)SULFANYL]-3-PENT-4-YN-1-YL-3H-PURIN-6-AMINE'>P54</scene></td></tr>
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</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=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=P54:8-[(2,4-DIMETHYLPHENYL)SULFANYL]-3-PENT-4-YN-1-YL-3H-PURIN-6-AMINE'>P54</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fwy|2fwy]], [[3o0i|3o0i]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fwy|2fwy]], [[3o0i|3o0i]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRP94, HSP90B1, TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 CANLF])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRP94, HSP90B1, TRA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 CANLF])</td></tr>
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<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=3o2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o2f OCA], [http://pdbe.org/3o2f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o2f RCSB], [http://www.ebi.ac.uk/pdbsum/3o2f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o2f ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o2f OCA], [https://pdbe.org/3o2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o2f RCSB], [https://www.ebi.ac.uk/pdbsum/3o2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o2f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ENPL_CANFA ENPL_CANFA]] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity).
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[[https://www.uniprot.org/uniprot/ENPL_CANFA ENPL_CANFA]] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 3o2f" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3o2f" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Canlf]]
[[Category: Canlf]]
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[[Category: Large Structures]]
[[Category: Gewirth, D T]]
[[Category: Gewirth, D T]]
[[Category: Seidler, P M]]
[[Category: Seidler, P M]]
[[Category: Chaperone-inhibitor complex]]
[[Category: Chaperone-inhibitor complex]]
[[Category: Hsp90 heat-shock protein]]
[[Category: Hsp90 heat-shock protein]]

Revision as of 07:14, 12 May 2022

Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54

PDB ID 3o2f

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