3o2f: Difference between revisions
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==Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54== | |||
<StructureSection load='3o2f' size='340' side='right'caption='[[3o2f]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3o2f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. 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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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> | ||
<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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ENPL_CANLF ENPL_CANLF] 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). | |||
== | ==See Also== | ||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[ | |||
[[Category: Canis lupus familiaris]] | [[Category: Canis lupus familiaris]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Gewirth DT]] | ||
[[Category: | [[Category: Seidler PM]] | ||
Latest revision as of 13:02, 14 February 2024
Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54
Structural highlights
FunctionENPL_CANLF 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). See Also |
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