6nb1
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Escherichia coli ClpP protease complexed with small molecule activator, ACP1-06== | |
| - | + | <StructureSection load='6nb1' size='340' side='right'caption='[[6nb1]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6nb1]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NB1 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KHS:N-{2-[(2-chlorophenyl)sulfanyl]ethyl}-2-methyl-2-{[5-(trifluoromethyl)pyridin-2-yl]sulfonyl}propanamide'>KHS</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6nb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nb1 OCA], [http://pdbe.org/6nb1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nb1 RCSB], [http://www.ebi.ac.uk/pdbsum/6nb1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nb1 ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Endopeptidase Clp]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Bryson, S]] | [[Category: Bryson, S]] | ||
| - | [[Category: Houry, W | + | [[Category: Eger, B T]] |
| - | [[Category: Mabanglo, M | + | [[Category: Houry, W A]] |
| - | [[Category: | + | [[Category: Mabanglo, M F]] |
| + | [[Category: Pai, E F]] | ||
| + | [[Category: Antibiotic]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Serine protease]] | ||
Revision as of 11:05, 13 November 2019
Crystal structure of Escherichia coli ClpP protease complexed with small molecule activator, ACP1-06
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