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3p2l
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3p2l is ON HOLD Authors: Kim, Y., Zhou, M., Papazisi, L., Anderson, W.F., Joachimiak, A., CSGID, Center for Structural Genomics of Infectious Diseas...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis== | |
| + | <StructureSection load='3p2l' size='340' side='right'caption='[[3p2l]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3p2l]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis_subsp._tularensis_SCHU_S4 Francisella tularensis subsp. tularensis SCHU S4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P2L FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.295Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=3p2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p2l OCA], [https://pdbe.org/3p2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p2l RCSB], [https://www.ebi.ac.uk/pdbsum/3p2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p2l ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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] | ||
| - | + | ==See Also== | |
| - | + | *[[Clp protease 3D structures|Clp protease 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Francisella tularensis subsp. tularensis SCHU S4]] | |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Anderson WF]] | ||
| + | [[Category: Gu M]] | ||
| + | [[Category: Joachimiak A]] | ||
| + | [[Category: Kim Y]] | ||
| + | [[Category: Zhou M]] | ||
Current revision
Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis
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