3gdq

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==Crystal structure of the human 70kDa heat shock protein 1-like ATPase domain in complex with ADP and inorganic phosphate==
==Crystal structure of the human 70kDa heat shock protein 1-like ATPase domain in complex with ADP and inorganic phosphate==
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<StructureSection load='3gdq' size='340' side='right' caption='[[3gdq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='3gdq' size='340' side='right'caption='[[3gdq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3gdq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GDQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3gdq]] 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=3GDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GDQ 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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPA1L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=3gdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gdq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gdq RCSB], [http://www.ebi.ac.uk/pdbsum/3gdq PDBsum]</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=3gdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gdq OCA], [https://pdbe.org/3gdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gdq RCSB], [https://www.ebi.ac.uk/pdbsum/3gdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gdq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HS71L_HUMAN HS71L_HUMAN]] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity).
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[https://www.uniprot.org/uniprot/HS71L_HUMAN HS71L_HUMAN] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gd/3gdq_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gd/3gdq_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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</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=3gdq ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3gdq" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Heat Shock Proteins|Heat Shock Proteins]]
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C H]]
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[[Category: Large Structures]]
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[[Category: Berg, S Van Den]]
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[[Category: Arrowsmith CH]]
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[[Category: Berglund, H]]
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[[Category: Berglund H]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Collins, R]]
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[[Category: Collins R]]
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[[Category: Dahlgren, L G]]
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[[Category: Dahlgren LG]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Flodin, S]]
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[[Category: Flodin S]]
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[[Category: Flores, A]]
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[[Category: Flores A]]
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[[Category: Graslund, S]]
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[[Category: Graslund S]]
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[[Category: Hammarstrom, M]]
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[[Category: Hammarstrom M]]
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[[Category: Johansson, A]]
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[[Category: Johansson A]]
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[[Category: Johansson, I]]
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[[Category: Johansson I]]
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[[Category: Karlberg, T]]
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[[Category: Karlberg T]]
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[[Category: Kotenyova, T]]
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[[Category: Kotenyova T]]
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[[Category: Lehtio, L]]
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[[Category: Lehtio L]]
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[[Category: Moche, M]]
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[[Category: Moche M]]
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[[Category: Nilsson, M E]]
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[[Category: Nilsson ME]]
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[[Category: Nordlund, P]]
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[[Category: Nordlund P]]
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[[Category: Nyman, T]]
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[[Category: Nyman T]]
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[[Category: Persson, C]]
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[[Category: Persson C]]
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[[Category: Structural genomic]]
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[[Category: Sagemark J]]
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[[Category: Sagemark, J]]
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[[Category: Schueler H]]
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[[Category: Schueler, H]]
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[[Category: Schutz P]]
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[[Category: Schutz, P]]
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[[Category: Siponen M]]
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[[Category: Siponen, M]]
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[[Category: Thorsell AG]]
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[[Category: Thorsell, A G]]
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[[Category: Tresaugues L]]
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[[Category: Tresaugues, L]]
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[[Category: Van Den Berg S]]
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[[Category: Weigelt, J]]
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[[Category: Weigelt J]]
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[[Category: Welin, M]]
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[[Category: Welin M]]
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[[Category: Wisniewska, M]]
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[[Category: Wisniewska M]]
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[[Category: Atp-binding]]
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[[Category: Chaperone]]
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[[Category: Helix]]
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[[Category: Nucleotide-binding]]
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[[Category: Sgc]]
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[[Category: Transcription]]
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Current revision

Crystal structure of the human 70kDa heat shock protein 1-like ATPase domain in complex with ADP and inorganic phosphate

PDB ID 3gdq

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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