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2zl2

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==Crystal structure of H.pylori ClpP in complex with the peptide NVLGFTQ==
==Crystal structure of H.pylori ClpP in complex with the peptide NVLGFTQ==
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<StructureSection load='2zl2' size='340' side='right' caption='[[2zl2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='2zl2' size='340' side='right'caption='[[2zl2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2zl2]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZL2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2zl2]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZL2 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zl0|2zl0]], [[2zl3|2zl3]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zl0|2zl0]], [[2zl3|2zl3]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zl2 OCA], [http://pdbe.org/2zl2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zl2 RCSB], [http://www.ebi.ac.uk/pdbsum/2zl2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zl2 ProSAT]</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=2zl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zl2 OCA], [https://pdbe.org/2zl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zl2 RCSB], [https://www.ebi.ac.uk/pdbsum/2zl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zl2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CLPP_HELPY CLPP_HELPY]] 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_HELPY CLPP_HELPY]] 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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Clp Protease|Clp Protease]]
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*[[Clp protease 3D structures|Clp protease 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Atcc 43504]]
[[Category: Atcc 43504]]
[[Category: Endopeptidase Clp]]
[[Category: Endopeptidase Clp]]
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[[Category: Large Structures]]
[[Category: Kim, D Y]]
[[Category: Kim, D Y]]
[[Category: Kim, K K]]
[[Category: Kim, K K]]

Revision as of 17:32, 15 December 2021

Crystal structure of H.pylori ClpP in complex with the peptide NVLGFTQ

PDB ID 2zl2

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