7dfu

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Current revision (16:32, 29 November 2023) (edit) (undo)
 
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<StructureSection load='7dfu' size='340' side='right'caption='[[7dfu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='7dfu' size='340' side='right'caption='[[7dfu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7dfu]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/"pseudomonas_oryzae"_uyeda_and_ishiyama_in_ishiyama_1926 "pseudomonas oryzae" uyeda and ishiyama in ishiyama 1926]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DFU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7dfu]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_oryzae Xanthomonas oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DFU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EZA:N-[(6aS,12S,15aS,17R,21R,23aS)-17,21-dimethyl-6,11,15,20,23-pentaoxooctadecahydro-2H,6H,11H,15H-pyrido[2,1-i]dipyrrolo[2,1-c 2,1-l][1,4,7,10,13]oxatetraazacyclohexadecin-12-yl]-3,5-difluoro-Nalpha-[(2E)-hept-2-enoyl]-L-phenylalaninamide'>EZA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.901&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP, ADT25_23080, ADT27_15185, EYR26_04825 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=347 "Pseudomonas oryzae" Uyeda and Ishiyama in Ishiyama 1926])</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EZA:N-[(6aS,12S,15aS,17R,21R,23aS)-17,21-dimethyl-6,11,15,20,23-pentaoxooctadecahydro-2H,6H,11H,15H-pyrido[2,1-i]dipyrrolo[2,1-c 2,1-l][1,4,7,10,13]oxatetraazacyclohexadecin-12-yl]-3,5-difluoro-Nalpha-[(2E)-hept-2-enoyl]-L-phenylalaninamide'>EZA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=7dfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dfu OCA], [https://pdbe.org/7dfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dfu RCSB], [https://www.ebi.ac.uk/pdbsum/7dfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dfu ProSAT]</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=7dfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dfu OCA], [https://pdbe.org/7dfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dfu RCSB], [https://www.ebi.ac.uk/pdbsum/7dfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dfu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/A0A0M1K022_9XANT A0A0M1K022_9XANT]] 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]
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[https://www.uniprot.org/uniprot/CLPP_XANOR CLPP_XANOR] 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]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Pseudomonas oryzae uyeda and ishiyama in ishiyama 1926]]
 
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[[Category: Endopeptidase Clp]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Yang, C G]]
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[[Category: Xanthomonas oryzae]]
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[[Category: Yang, T]]
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[[Category: Yang C-G]]
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[[Category: Caseinolytic protease p]]
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[[Category: Yang T]]
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[[Category: Clp protease]]
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[[Category: Hydrolase]]
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Current revision

Crystal structure of Xanthomonas oryzae ClpP S68Y in complex with ADEP4.

PDB ID 7dfu

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OCA

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