6mx2: Difference between revisions

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<StructureSection load='6mx2' size='340' side='right'caption='[[6mx2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='6mx2' size='340' side='right'caption='[[6mx2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[6mx2]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile_630 Clostridioides difficile 630]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6mx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mx2 OCA], [https://pdbe.org/6mx2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mx2 RCSB], [https://www.ebi.ac.uk/pdbsum/6mx2 PDBsum], [https://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>
</table>
</table>
== 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]  
[https://www.uniprot.org/uniprot/Q180F0_CLOD6 Q180F0_CLOD6] 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]


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Clod6]]
[[Category: Clostridioides difficile 630]]
[[Category: Endopeptidase Clp]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Duerfeldt, A S]]
[[Category: Duerfeldt AS]]
[[Category: Lavey, N P]]
[[Category: Lavey NP]]
[[Category: Thomas, L M]]
[[Category: Thomas LM]]
[[Category: Casinolytic protease tetradecamer clostridium difficule]]
[[Category: Hydrolase]]

Latest revision as of 09:40, 11 October 2023

Crystal Structure of ClpP1 from Clostridium difficile 630.Crystal Structure of ClpP1 from Clostridium difficile 630.

Structural highlights

6mx2 is a 14 chain structure with sequence from Clostridioides difficile 630. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q180F0_CLOD6 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]

See Also

6mx2, resolution 2.50Å

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