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4u0g

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==Crystal Structure of M. tuberculosis ClpP1P2 bound to ADEP and agonist==
==Crystal Structure of M. tuberculosis ClpP1P2 bound to ADEP and agonist==
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<StructureSection load='4u0g' size='340' side='right' caption='[[4u0g]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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<StructureSection load='4u0g' size='340' side='right'caption='[[4u0g]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4u0g]] is a 42 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U0G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4u0g]] is a 42 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv] 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=4U0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U0G 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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZIL:N-[(BENZYLOXY)CARBONYL]-L-ISOLEUCYL-L-LEUCINE'>ZIL</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]] 3.1978&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=39Y:(2E,5S)-5-METHYLHEPT-2-ENOIC+ACID'>39Y</scene>, <scene name='pdbligand=3A0:(2S,4S)-4-METHYLPIPERIDINE-2-CARBOXYLIC+ACID'>3A0</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=WFP:3,5-DIFLUORO-L-PHENYLALANINE'>WFP</scene></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=39Y:(2E,5S)-5-METHYLHEPT-2-ENOIC+ACID'>39Y</scene>, <scene name='pdbligand=3A0:(2S,4S)-4-METHYLPIPERIDINE-2-CARBOXYLIC+ACID'>3A0</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=WFP:3,5-DIFLUORO-L-PHENYLALANINE'>WFP</scene>, <scene name='pdbligand=ZIL:N-[(BENZYLOXY)CARBONYL]-L-ISOLEUCYL-L-LEUCINE'>ZIL</scene></td></tr>
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<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>
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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=4u0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0g OCA], [https://pdbe.org/4u0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u0g RCSB], [https://www.ebi.ac.uk/pdbsum/4u0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u0g ProSAT]</span></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=4u0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u0g RCSB], [http://www.ebi.ac.uk/pdbsum/4u0g PDBsum]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://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).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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 4u0g" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Clp protease 3D structures|Clp protease 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Endopeptidase Clp]]
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[[Category: Large Structures]]
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[[Category: Carney, D W]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Sauer, R T]]
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[[Category: Synthetic construct]]
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[[Category: Schmitz, K R]]
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[[Category: Carney DW]]
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[[Category: Sello, J K]]
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[[Category: Sauer RT]]
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[[Category: Hydrolase]]
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[[Category: Schmitz KR]]
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[[Category: Hydrolase-antibiotic complex]]
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[[Category: Sello JK]]
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[[Category: Peptidase]]
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Current revision

Crystal Structure of M. tuberculosis ClpP1P2 bound to ADEP and agonist

PDB ID 4u0g

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