6nah
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Neisseria meningitidis ClpP protease in complex with Acyldepsipeptide-14 (ADEP-14)== | |
| - | + | <StructureSection load='6nah' size='340' side='right'caption='[[6nah]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6nah]] is a 56 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NAH FirstGlance]. <br> | |
| - | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALO:ALLO-THREONINE'>ALO</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=OCA:OCTANOIC+ACID+(CAPRYLIC+ACID)'>OCA</scene>, <scene name='pdbligand=WFP:3,5-DIFLUORO-L-PHENYLALANINE'>WFP</scene>, <scene name='pdbligand=YCP:(2S)-PIPERIDINE-2-CARBOXYLIC+ACID'>YCP</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: Houry, W | + | <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=6nah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nah OCA], [http://pdbe.org/6nah PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nah RCSB], [http://www.ebi.ac.uk/pdbsum/6nah PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nah ProSAT]</span></td></tr> |
| - | [[Category: Mabanglo, M | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/I4E574_NEIME I4E574_NEIME]] 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][RuleBase:RU000550][SAAS:SAAS00674840] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Endopeptidase Clp]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Houry, W A]] | ||
| + | [[Category: Mabanglo, M F]] | ||
| + | [[Category: Antibiotic]] | ||
| + | [[Category: Anticancer]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
| + | [[Category: Serine protease]] | ||
Revision as of 11:05, 13 November 2019
Crystal structure of Neisseria meningitidis ClpP protease in complex with Acyldepsipeptide-14 (ADEP-14)
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