1ats
From Proteopedia
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| - | [[Image:1ats.png|left|200px]] | ||
| - | + | ==THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS== | |
| - | + | <StructureSection load='1ats' size='340' side='right'caption='[[1ats]], [[Resolution|resolution]] 2.43Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1ats]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ATS 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]] 2.43Å</td></tr> | |
| - | + | <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=MG:MAGNESIUM+ION'>MG</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=1ats FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ats OCA], [https://pdbe.org/1ats PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ats RCSB], [https://www.ebi.ac.uk/pdbsum/1ats PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ats ProSAT]</span></td></tr> |
| - | [[1ats]] is a 1 chain structure | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HSP7C_BOVIN HSP7C_BOVIN] Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (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/at/1ats_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=1ats ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Heat Shock | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | + | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Mckay | + | [[Category: Mckay DB]] |
| - | [[Category: | + | [[Category: O'Brien MC]] |
Current revision
THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS
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