3hln
From Proteopedia
(Difference between revisions)
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==Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds== | ==Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds== | ||
- | <StructureSection load='3hln' size='340' side='right' caption='[[3hln]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='3hln' size='340' side='right'caption='[[3hln]], [[Resolution|resolution]] 3.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3hln]] is a 28 chain structure with sequence from [ | + | <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> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </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> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0437, clpP, JW0427, lopP ([ | + | <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> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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 == | ||
- | [[ | + | [[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 | + | *[[Clp protease 3D structures|Clp protease 3D structures]] |
- | + | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Ecoli]] | [[Category: Ecoli]] | ||
[[Category: Endopeptidase Clp]] | [[Category: Endopeptidase Clp]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Borg, M]] | [[Category: Borg, M]] | ||
[[Category: Chan, H S]] | [[Category: Chan, H S]] |
Revision as of 12:01, 13 October 2021
Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds
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