5dzk
From Proteopedia
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==Crystal structure of the active form of the proteolytic complex clpP1 and clpP2== | ==Crystal structure of the active form of the proteolytic complex clpP1 and clpP2== | ||
| - | <StructureSection load='5dzk' size='340' side='right' caption='[[5dzk]], [[Resolution|resolution]] 3.07Å' scene=''> | + | <StructureSection load='5dzk' size='340' side='right'caption='[[5dzk]], [[Resolution|resolution]] 3.07Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5dzk]] is a 56 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DZK OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[5dzk]] is a 56 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycto Mycto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DZK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DZK FirstGlance]. <br> |
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP2, MT2535 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83331 MYCTO]), clpP1, clpP, MT2536 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83331 MYCTO])</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='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'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5dzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dzk OCA], [http://pdbe.org/5dzk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dzk RCSB], [http://www.ebi.ac.uk/pdbsum/5dzk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dzk ProSAT]</span></td></tr> |
</table> | </table> | ||
| - | {{Large structure}} | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CLPP2_MYCTO CLPP2_MYCTO]] 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] [[http://www.uniprot.org/uniprot/CLPP1_MYCTO CLPP1_MYCTO]] 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] | [[http://www.uniprot.org/uniprot/CLPP2_MYCTO CLPP2_MYCTO]] 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] [[http://www.uniprot.org/uniprot/CLPP1_MYCTO CLPP1_MYCTO]] 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] | ||
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</div> | </div> | ||
<div class="pdbe-citations 5dzk" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5dzk" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Clp protease 3D structures|Clp protease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Endopeptidase Clp]] | [[Category: Endopeptidase Clp]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycto]] | ||
[[Category: LI, M]] | [[Category: LI, M]] | ||
[[Category: Maurizi, M]] | [[Category: Maurizi, M]] | ||
[[Category: Wlodawer, A]] | [[Category: Wlodawer, A]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 08:15, 15 April 2020
Crystal structure of the active form of the proteolytic complex clpP1 and clpP2
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