3mt6: Difference between revisions
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==Structure of ClpP from Escherichia coli in complex with ADEP1== | ==Structure of ClpP from Escherichia coli in complex with ADEP1== | ||
<StructureSection load='3mt6' size='340' side='right' caption='[[3mt6]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3mt6' size='340' side='right'caption='[[3mt6]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3mt6]] is a 56 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3mt6]] is a 56 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli] and [https://en.wikipedia.org/wiki/Streptomyces_hawaiiensis Streptomyces hawaiiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MT6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAA:N-METHYL-L-ALANINE'>MAA</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=OTT:(2E,4E,6E)-OCTA-2,4,6-TRIENOIC+ACID'>OTT</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAA:N-METHYL-L-ALANINE'>MAA</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=OTT:(2E,4E,6E)-OCTA-2,4,6-TRIENOIC+ACID'>OTT</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yg6|1yg6]], [[3ktg|3ktg]], [[3kth|3kth]], [[3kti|3kti]], [[3ktj|3ktj]], [[3ktk|3ktk]], [[1tyf|1tyf]], [[2fzs|2fzs]], [[1y7o|1y7o]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yg6|1yg6]], [[3ktg|3ktg]], [[3kth|3kth]], [[3kti|3kti]], [[3ktj|3ktj]], [[3ktk|3ktk]], [[1tyf|1tyf]], [[2fzs|2fzs]], [[1y7o|1y7o]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0437, clpP, JW0427, lopP ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0437, clpP, JW0427, lopP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mt6 OCA], [https://pdbe.org/3mt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mt6 RCSB], [https://www.ebi.ac.uk/pdbsum/3mt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mt6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CLPP_ECOLI CLPP_ECOLI]] 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Clp | *[[Clp protease 3D structures|Clp protease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Ecoli]] | [[Category: Ecoli]] | ||
[[Category: Endopeptidase Clp]] | [[Category: Endopeptidase Clp]] | ||
[[Category: Large Structures]] | |||
[[Category: Streptomyces hawaiiensis]] | [[Category: Streptomyces hawaiiensis]] | ||
[[Category: Chung, Y S]] | [[Category: Chung, Y S]] |