2fyp
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2fyp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fyp, resolution 1.95Å" /> '''GRP94 in complex wit...) |
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| - | [[Image:2fyp.jpg|left|200px]]<br /><applet load="2fyp" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2fyp, resolution 1.95Å" /> | ||
| - | '''GRP94 in complex with the novel HSP90 Inhibitor Radester amine'''<br /> | ||
| - | == | + | ==GRP94 in complex with the novel HSP90 Inhibitor Radester amine== |
| - | + | <StructureSection load='2fyp' size='340' side='right'caption='[[2fyp]], [[Resolution|resolution]] 1.95Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2fyp]] 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=2FYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FYP 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]] 1.95Å</td></tr> |
| - | [[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=RDE:2-(3-AMINO-2,5,6-TRIMETHOXYPHENYL)ETHYL+5-CHLORO-2,4-DIHYDROXYBENZOATE'>RDE</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=2fyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fyp OCA], [https://pdbe.org/2fyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fyp RCSB], [https://www.ebi.ac.uk/pdbsum/2fyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fyp 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). |
| - | [ | + | == Evolutionary Conservation == |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | [ | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/2fyp_consurf.spt"</scriptWhenChecked> |
| - | [[ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | [ | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | [[ | + | </jmolCheckbox> |
| - | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fyp ConSurf]. | |
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Canis lupus familiaris]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gewirth DT]] | ||
| + | [[Category: Immormino RM]] | ||
Current revision
GRP94 in complex with the novel HSP90 Inhibitor Radester amine
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