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9p9v

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Current revision (07:46, 19 November 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9p9v is ON HOLD until Paper Publication
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==Human ClpX initial assembly==
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<StructureSection load='9p9v' size='340' side='right'caption='[[9p9v]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
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Authors: Chen, W.C.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9p9v]] is a 6 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=9P9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9P9V FirstGlance]. <br>
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Description: Human ClpX initial assembly
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.4&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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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></td></tr>
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[[Category: Chen, W.C]]
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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=9p9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9p9v OCA], [https://pdbe.org/9p9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9p9v RCSB], [https://www.ebi.ac.uk/pdbsum/9p9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9p9v ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CLPX_HUMAN CLPX_HUMAN] The disease may be caused by variants affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/CLPX_HUMAN CLPX_HUMAN] ATP-dependent chaperone that functions as an unfoldase. As part of the ClpXP protease complex, it recognizes specific protein substrates, unfolds them using energy derived from ATP hydrolysis, and then translocates them to the proteolytic subunit (CLPP) of the ClpXP complex for degradation (PubMed:11923310, PubMed:22710082, PubMed:28874591). Thanks to its chaperone activity, it also functions in the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis (PubMed:28874591). This chaperone is also involved in the control of mtDNA nucleoid distribution, by regulating mitochondrial transcription factor A (TFAM) activity (PubMed:22841477).<ref>PMID:11923310</ref> <ref>PMID:22710082</ref> <ref>PMID:22841477</ref> <ref>PMID:28874591</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Chen WC]]

Current revision

Human ClpX initial assembly

PDB ID 9p9v

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