6nah: Difference between revisions

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<StructureSection load='6nah' size='340' side='right'caption='[[6nah]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='6nah' size='340' side='right'caption='[[6nah]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6nah]] is a 56 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887]. 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>
<table><tr><td colspan='2'>[[6nah]] is a 56 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. 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 [https://proteopedia.org/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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 "Diplokokkus intracellularis meningitidis" (sic) Weichselbaum 1887])</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=6nah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nah OCA], [https://pdbe.org/6nah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nah RCSB], [https://www.ebi.ac.uk/pdbsum/6nah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nah ProSAT]</span></td></tr>
<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=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>
</table>
</table>
== Function ==
== 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]  
[https://www.uniprot.org/uniprot/CLPP_NEIMB CLPP_NEIMB] 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]
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
<div class="pdbe-citations 6nah" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6nah" style="background-color:#fffaf0;"></div>
==See Also==
*[[Clp protease 3D structures|Clp protease 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Endopeptidase Clp]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Houry, W A]]
[[Category: Neisseria meningitidis]]
[[Category: Mabanglo, M F]]
[[Category: Synthetic construct]]
[[Category: Antibiotic]]
[[Category: Houry WA]]
[[Category: Anticancer]]
[[Category: Mabanglo MF]]
[[Category: Hydrolase]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Serine protease]]

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