6naq: Difference between revisions

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'''Unreleased structure'''


The entry 6naq is ON HOLD  until Paper Publication
==Crystal structure of Neisseria meningitidis ClpP protease in Apo form==
 
<StructureSection load='6naq' size='340' side='right'caption='[[6naq]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
Authors: Houry, W.A., Mabanglo, M.F., Pai, E.F., Eger, B.T., Bryson, S.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6naq]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NAQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NAQ FirstGlance]. <br>
Description: Crystal structure of Neisseria meningitidis ClpP protease in Apo form
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6nah|6nah]]</td></tr>
[[Category: Pai, E.F]]
<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>
<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=6naq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6naq OCA], [http://pdbe.org/6naq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6naq RCSB], [http://www.ebi.ac.uk/pdbsum/6naq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6naq ProSAT]</span></td></tr>
</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: Bryson, S]]
[[Category: Bryson, S]]
[[Category: Mabanglo, M.F]]
[[Category: Eger, B T]]
[[Category: Eger, B.T]]
[[Category: Houry, W A]]
[[Category: Houry, W.A]]
[[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 Neisseria meningitidis ClpP protease in Apo form

6naq, resolution 2.02Å

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