4ryf: Difference between revisions

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-'''Unreleased structure'''
+==ClpP1/2 heterocomplex from Listeria monocytogenes==
+<StructureSection load='4ryf' size='340' side='right' caption='[[4ryf]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-The entry 4ryf is ON HOLD
+== 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>
-Authors: Dahmen, M., Vielberg, M.-T., Groll, M., Sieber, S. A.
+</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>
-Description: ClpP1/2 heterocomplex from Listeria monocytogenes
+<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: Unreleased Structures]]
+<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: Vielberg, M.-T]]
-[[Category: Sieber, S. A]]
 [[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]]