6pka

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Current revision (07:31, 11 October 2023) (edit) (undo)
 
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<StructureSection load='6pka' size='340' side='right'caption='[[6pka]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='6pka' size='340' side='right'caption='[[6pka]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6pka]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PKA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PKA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6pka]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PKA FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=OO1:'>OO1</scene>, <scene name='pdbligand=WFP:3,5-DIFLUORO-L-PHENYLALANINE'>WFP</scene>, <scene name='pdbligand=YCP:(2S)-PIPERIDINE-2-CARBOXYLIC+ACID'>YCP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vz2|5vz2]], [[5w18|5w18]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=OO1:(4-methylphenyl)carbamic+acid'>OO1</scene>, <scene name='pdbligand=PRD_002359:OO1-WFP-SER-PRO-YCP-ALA-MP8+ureadepsipeptide'>PRD_002359</scene>, <scene name='pdbligand=WFP:3,5-DIFLUORO-L-PHENYLALANINE'>WFP</scene>, <scene name='pdbligand=YCP:(2S)-PIPERIDINE-2-CARBOXYLIC+ACID'>YCP</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP, SAOUHSC_00790 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93061 STAA8])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pka OCA], [https://pdbe.org/6pka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pka RCSB], [https://www.ebi.ac.uk/pdbsum/6pka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pka ProSAT]</span></td></tr>
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<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>
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<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=6pka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pka OCA], [http://pdbe.org/6pka PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pka RCSB], [http://www.ebi.ac.uk/pdbsum/6pka PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pka ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CLPP_STAA8 CLPP_STAA8]] 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).
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[https://www.uniprot.org/uniprot/CLPP_STAA8 CLPP_STAA8] 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).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6pka" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6pka" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Clp protease 3D structures|Clp protease 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Endopeptidase Clp]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Staa8]]
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[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]]
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[[Category: Griffith, E C]]
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[[Category: Synthetic construct]]
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[[Category: Lee, R E]]
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[[Category: Griffith EC]]
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[[Category: Antibiotic]]
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[[Category: Lee RE]]
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[[Category: Clpp adep]]
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[[Category: Hydrolase-antibiotic complex]]
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Current revision

Structure of ClpP from Staphylococcus aureus in complex with ureadepsipeptide

PDB ID 6pka

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