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==Crystal Structure of ClpP1 from Clostridium | ==Crystal Structure of ClpP1 from Clostridium difficile 630.== | ||
<StructureSection load='6mx2' size='340' side='right' caption='[[6mx2]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='6mx2' size='340' side='right'caption='[[6mx2]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6mx2]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MX2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MX2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6mx2]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Clod6 Clod6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MX2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MX2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP1, clpP, CD630_33050 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272563 CLOD6])</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mx2 OCA], [http://pdbe.org/6mx2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mx2 RCSB], [http://www.ebi.ac.uk/pdbsum/6mx2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mx2 ProSAT]</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=6mx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mx2 OCA], [http://pdbe.org/6mx2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mx2 RCSB], [http://www.ebi.ac.uk/pdbsum/6mx2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mx2 ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/Q180F0_PEPD6 Q180F0_PEPD6]] 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][RuleBase:RU000550][SAAS:SAAS00674840] | [[http://www.uniprot.org/uniprot/Q180F0_PEPD6 Q180F0_PEPD6]] 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][RuleBase:RU000550][SAAS:SAAS00674840] | ||
==See Also== | |||
*[[Clp protease 3D structures|Clp protease 3D structures]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Clod6]] | |||
[[Category: Endopeptidase Clp]] | [[Category: Endopeptidase Clp]] | ||
[[Category: Large Structures]] | |||
[[Category: Duerfeldt, A S]] | [[Category: Duerfeldt, A S]] | ||
[[Category: Lavey, N P]] | [[Category: Lavey, N P]] | ||
Revision as of 14:31, 1 January 2020
Crystal Structure of ClpP1 from Clostridium difficile 630.Crystal Structure of ClpP1 from Clostridium difficile 630.
Structural highlights
Function[Q180F0_PEPD6] 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][RuleBase:RU000550][SAAS:SAAS00674840] See Also |
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