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4ryf
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==ClpP1/2 heterocomplex from Listeria monocytogenes== |
| - | + | <StructureSection load='4ryf' size='340' side='right' caption='[[4ryf]], [[Resolution|resolution]] 2.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4ryf]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RYF FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fzs|2fzs]], [[4jcq|4jcq]], [[4jct|4jct]]</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=4ryf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ryf RCSB], [http://www.ebi.ac.uk/pdbsum/4ryf PDBsum]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/Q8Y7Y1_LISMO Q8Y7Y1_LISMO]] 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).[HAMAP-Rule:MF_00444] [[http://www.uniprot.org/uniprot/CLPP_LISMO CLPP_LISMO]] 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). | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Endopeptidase Clp]] | ||
[[Category: Dahmen, M]] | [[Category: Dahmen, M]] | ||
| - | [[Category: Vielberg, M.-T]] | ||
| - | [[Category: Sieber, S. A]] | ||
[[Category: Groll, M]] | [[Category: Groll, M]] | ||
| + | [[Category: Sieber, S A]] | ||
| + | [[Category: Vielberg, M T]] | ||
| + | [[Category: Clpp]] | ||
| + | [[Category: Enzyme catalysis]] | ||
| + | [[Category: Heterocomplex]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Pathogenic bacteria]] | ||
| + | [[Category: Proteolysis]] | ||
| + | [[Category: Ser-protease]] | ||
Revision as of 14:54, 31 December 2014
ClpP1/2 heterocomplex from Listeria monocytogenes
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