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3o2f
From Proteopedia
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| - | {{STRUCTURE_3o2f| PDB=3o2f | SCENE= }} | ||
| - | ===Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54=== | ||
| - | {{ABSTRACT_PUBMED_23995768}} | ||
| - | == | + | ==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> |
| - | [[3o2f]] is a 2 chain structure with sequence from [ | + | </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== | ==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]] |
| - | + | ||
Current revision
Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54
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