3kth: Difference between revisions

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 ==Structure of ClpP from Bacillus subtilis in orthorombic crystal form==
-<StructureSection load='3kth' size='340' side='right' caption='[[3kth]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+<StructureSection load='3kth' size='340' side='right'caption='[[3kth]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3kth]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KTH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KTH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3kth]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KTH FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ktg|3ktg]], [[3kti|3kti]], [[3ktj|3ktj]], [[3ktk|3ktk]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP, yvdN, BSU34540 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</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=3kth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kth OCA], [https://pdbe.org/3kth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kth RCSB], [https://www.ebi.ac.uk/pdbsum/3kth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kth ProSAT]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kth OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kth RCSB], [http://www.ebi.ac.uk/pdbsum/3kth PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CLPP_BACSU CLPP_BACSU]] 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). ClpXP is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor.<ref>PMID:16899079</ref>
+[https://www.uniprot.org/uniprot/CLPP_BACSU CLPP_BACSU] 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). ClpXP is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor.<ref>PMID:16899079</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kt/3kth_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kt/3kth_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3kth ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3kth" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Clp Protease|Clp Protease]]
+*[[Clp protease 3D structures|Clp protease 3D structures]]
 == References ==
 <references/>
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Bacillus subtilis]]
-[[Category: Endopeptidase Clp]]
+[[Category: Large Structures]]
-[[Category: Brotz-Oesterhelt, H]]
+[[Category: Brotz-Oesterhelt H]]
-[[Category: Lee, B G]]
+[[Category: Lee B-G]]
-[[Category: Song, H K]]
+[[Category: Song HK]]
-[[Category: Atp-binding]]
-[[Category: Hydrolase]]
-[[Category: Nucleotide-binding]]
-[[Category: Protease]]
-[[Category: Serine protease]]
-[[Category: Stress response]]