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7mk5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Escherichia coli ClpP covalently inhibited by clipibicyclene== | |
| + | <StructureSection load='7mk5' size='340' side='right'caption='[[7mk5]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7mk5]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MK5 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]] 2.95Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZGV:4-[(1E)-3-{[(2E,4E,6E,8S)-8-hydroxy-4-methyldeca-2,4,6-trienoyl]amino}-3-oxoprop-1-en-1-yl]azete-1(2H)-carboxylic+acid'>ZGV</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=7mk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mk5 OCA], [https://pdbe.org/7mk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mk5 RCSB], [https://www.ebi.ac.uk/pdbsum/7mk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mk5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Clp protease 3D structures|Clp protease 3D structures]] | |
| - | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Culp EJ]] | ||
| + | [[Category: Hobson C]] | ||
| + | [[Category: Pawlowski AJ]] | ||
| + | [[Category: Prehna G]] | ||
| + | [[Category: Sychantha D]] | ||
| + | [[Category: Wright GD]] | ||
Current revision
Crystal structure of Escherichia coli ClpP covalently inhibited by clipibicyclene
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