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5g1s
From Proteopedia
(Difference between revisions)
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<StructureSection load='5g1s' size='340' side='right'caption='[[5g1s]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5g1s' size='340' side='right'caption='[[5g1s]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5g1s]] is a 21 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5g1s]] is a 21 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=5G1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G1S 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]] 1.7Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5g1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1s OCA], [https://pdbe.org/5g1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g1s RCSB], [https://www.ebi.ac.uk/pdbsum/5g1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1s 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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==See Also== | ==See Also== | ||
| - | *[[Clp | + | *[[Clp protease 3D structures|Clp protease 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Francisella tularensis]] |
| - | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Diaz-Saez | + | [[Category: Diaz-Saez L]] |
| - | [[Category: Hunter | + | [[Category: Hunter WN]] |
| - | [[Category: Pankov | + | [[Category: Pankov G]] |
| - | + | ||
Revision as of 13:35, 26 July 2023
Open conformation of Francisella tularensis ClpP at 1.7 A
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