6nah: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6nah is ~~ON HOLD until Paper Publication~~

==Crystal structure of Neisseria meningitidis ClpP protease in complex with Acyldepsipeptide-14 (ADEP-14)==

~~Authors~~: ~~Mabanglo~~, M.F., ~~Houry~~, W.A.

== 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 guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NAH FirstGlance].

~~Description~~: ~~Crystal structure of Neisseria meningitidis ClpP protease~~ in ~~complex with Acyldepsipeptide~~-~~14 (ADEP~~-~~14)~~

</td></tr><tr id='NonStdRes'><td class="sblockLbl">[[Non-Standard_Residue|NonStd Res:]]</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: ~~Unreleased~~ Structures]]

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

[[Category: Houry, W.A]]

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[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]</td></tr>

[[Category: Mabanglo, M.F]]

</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]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6nah is ON HOLD  until Paper Publication
+==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]] 2.70&Aring;' scene=''>
-Authors: Mabanglo, M.F., Houry, W.A.
+== 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>
-Description: Crystal structure of Neisseria meningitidis ClpP protease in complex with Acyldepsipeptide-14 (ADEP-14)
+</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: Unreleased Structures]]
+<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.A]]
+<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.F]]
+</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]]