5dkp: Difference between revisions

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<StructureSection load='5dkp' size='340' side='right'caption='[[5dkp]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
<StructureSection load='5dkp' size='340' side='right'caption='[[5dkp]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5dkp]] is a 56 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimb Neimb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DKP FirstGlance]. <br>
<table><tr><td colspan='2'>[[5dkp]] is a 56 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58] 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=5DKP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DKP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.381&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAA:N-METHYL-L-ALANINE'>MAA</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=OTT:(2E,4E,6E)-OCTA-2,4,6-TRIENOIC+ACID'>OTT</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MAA:N-METHYL-L-ALANINE'>MAA</scene>, <scene name='pdbligand=MP8:(4R)-4-METHYL-L-PROLINE'>MP8</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OTT:(2E,4E,6E)-OCTA-2,4,6-TRIENOIC+ACID'>OTT</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP, NMB1312 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122586 NEIMB])</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=5dkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dkp OCA], [https://pdbe.org/5dkp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dkp RCSB], [https://www.ebi.ac.uk/pdbsum/5dkp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dkp 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=5dkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dkp OCA], [http://pdbe.org/5dkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dkp RCSB], [http://www.ebi.ac.uk/pdbsum/5dkp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dkp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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]  
[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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Endopeptidase Clp]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Neimb]]
[[Category: Neisseria meningitidis MC58]]
[[Category: Batey, R A]]
[[Category: Synthetic construct]]
[[Category: Bryson, S]]
[[Category: Batey RA]]
[[Category: Eger, B T]]
[[Category: Bryson S]]
[[Category: Goodreid, J D]]
[[Category: Eger BT]]
[[Category: Gray-Owen, S D]]
[[Category: Goodreid JD]]
[[Category: Houry, W A]]
[[Category: Gray-Owen SD]]
[[Category: Janetzko, J]]
[[Category: Houry WA]]
[[Category: Leung, E]]
[[Category: Janetzko J]]
[[Category: Maria, J P.Santa]]
[[Category: Leung E]]
[[Category: Pai, E F]]
[[Category: Pai EF]]
[[Category: Walker, S]]
[[Category: Santa Maria Jr JP]]
[[Category: Wong, K]]
[[Category: Walker S]]
[[Category: Agonist]]
[[Category: Wong K]]
[[Category: Antimicrobial]]
[[Category: Degradation]]
[[Category: Hydrolase]]
[[Category: Hydrolase-antibiotic complex]]

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