5dzk
From Proteopedia
(Difference between revisions)
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| - | ''' | + | {{Large structure}} |
| - | + | ==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=''> | |
| - | + | == 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://oca.weizmann.ac.il/oca-docs/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> | |
| - | + | <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> | |
| - | [[Category: | + | <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=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]</span></td></tr> |
| + | </table> | ||
| + | {{Large structure}} | ||
| + | == 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] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Endopeptidase Clp]] | ||
| + | [[Category: LI, M]] | ||
[[Category: Maurizi, M]] | [[Category: Maurizi, M]] | ||
[[Category: Wlodawer, A]] | [[Category: Wlodawer, A]] | ||
| - | [[Category: | + | [[Category: Hydrolase]] |
Revision as of 02:54, 21 February 2016
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Crystal structure of the active form of the proteolytic complex clpP1 and clpP2
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