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<StructureSection load='6vgn' size='340' side='right'caption='[[6vgn]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='6vgn' size='340' side='right'caption='[[6vgn]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6vgn]] is a 21 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VGN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VGN FirstGlance]. <br>
<table><tr><td colspan='2'>[[6vgn]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VGN FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALO:ALLO-THREONINE'>ALO</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=R0M:'>R0M</scene>, <scene name='pdbligand=WFP:3,5-DIFLUORO-L-PHENYLALANINE'>WFP</scene>, <scene name='pdbligand=YCP:(2S)-PIPERIDINE-2-CARBOXYLIC+ACID'>YCP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6vgk|6vgk]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALO:ALLO-THREONINE'>ALO</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=R0M:(2E,4E)-hepta-2,4-dienoic+acid'>R0M</scene>, <scene name='pdbligand=WFP:3,5-DIFLUORO-L-PHENYLALANINE'>WFP</scene>, <scene name='pdbligand=YCP:(2S)-PIPERIDINE-2-CARBOXYLIC+ACID'>YCP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></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=6vgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vgn OCA], [https://pdbe.org/6vgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vgn RCSB], [https://www.ebi.ac.uk/pdbsum/6vgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vgn ProSAT]</span></td></tr>
<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=6vgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vgn OCA], [http://pdbe.org/6vgn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vgn RCSB], [http://www.ebi.ac.uk/pdbsum/6vgn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vgn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A0A045HBE0_MYCTX A0A045HBE0_MYCTX]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.[HAMAP-Rule:MF_00444][RuleBase:RU000550][SAAS:SAAS00674840] [[http://www.uniprot.org/uniprot/CLPP1_MYCTU CLPP1_MYCTU]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
[https://www.uniprot.org/uniprot/CLPP2_MYCTU CLPP2_MYCTU] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA.[HAMAP-Rule:MF_00444]<ref>PMID:20025669</ref> <ref>PMID:23314154</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Endopeptidase Clp]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kay, L E]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Ripstein, Z A]]
[[Category: Synthetic construct]]
[[Category: Rubinstein, J L]]
[[Category: Kay LE]]
[[Category: Vahidi, S]]
[[Category: Ripstein ZA]]
[[Category: Clpp]]
[[Category: Rubinstein JL]]
[[Category: Complex]]
[[Category: Vahidi S]]
[[Category: Hydrolase]]
[[Category: Hydrolase-antibiotic complex]]
[[Category: Protease]]
[[Category: Tuberculosis]]
Retrieved from "https://proteopedia.org/6vgn"