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3hln

From Proteopedia

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Current revision (07:23, 6 September 2023) (edit) (undo)
 
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<StructureSection load='3hln' size='340' side='right'caption='[[3hln]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='3hln' size='340' side='right'caption='[[3hln]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3hln]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HLN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3hln]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HLN 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=CA:CALCIUM+ION'>CA</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]] 3.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0437, clpP, JW0427, lopP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=CA:CALCIUM+ION'>CA</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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [https://pdbe.org/3hln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [https://www.ebi.ac.uk/pdbsum/3hln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hln 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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [https://pdbe.org/3hln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [https://www.ebi.ac.uk/pdbsum/3hln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hln ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CLPP_ECOLI CLPP_ECOLI]] 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.
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[https://www.uniprot.org/uniprot/CLPP_ECOLI CLPP_ECOLI] 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.
== 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==
*[[Clp protease 3D structures|Clp protease 3D structures]]
*[[Clp protease 3D structures|Clp protease 3D structures]]
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
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[[Category: Endopeptidase Clp]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Borg, M]]
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[[Category: Borg M]]
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[[Category: Chan, H S]]
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[[Category: Chan HS]]
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[[Category: Houry, W A]]
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[[Category: Houry WA]]
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[[Category: Kimber, M S]]
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[[Category: Kimber MS]]
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[[Category: Yu, A Y.H]]
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[[Category: Yu AYH]]
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[[Category: Atp-binding]]
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[[Category: Disordered equatorial loop]]
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[[Category: Disulfide bond]]
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[[Category: Hydrolase]]
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[[Category: Nucleotide-binding]]
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[[Category: Protease]]
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[[Category: Serine protease]]
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[[Category: Stress response]]
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[[Category: Zymogen]]
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Current revision

Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds

PDB ID 3hln

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