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5g1q
From Proteopedia
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==Compressed conformation of Francisella tularensis ClpP at 2.84 A== | ==Compressed conformation of Francisella tularensis ClpP at 2.84 A== | ||
| - | <StructureSection load='5g1q' size='340' side='right' caption='[[5g1q]], [[Resolution|resolution]] 2.84Å' scene=''> | + | <StructureSection load='5g1q' size='340' side='right'caption='[[5g1q]], [[Resolution|resolution]] 2.84Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5g1q]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1Q OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5g1q]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis Francisella tularensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G1Q FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.84Å</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=5g1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1q OCA], [https://pdbe.org/5g1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g1q RCSB], [https://www.ebi.ac.uk/pdbsum/5g1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1q ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/CLPP_FRATT CLPP_FRATT] 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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</div> | </div> | ||
<div class="pdbe-citations 5g1q" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5g1q" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Clp protease 3D structures|Clp protease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Francisella tularensis]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Diaz-Saez L]] |
| - | [[Category: | + | [[Category: Hunter WN]] |
Current revision
Compressed conformation of Francisella tularensis ClpP at 2.84 A
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