2nyr: Difference between revisions

<StructureSection load='2nyr' size='340' side='right'caption='[[2nyr]], [[Resolution|resolution]] 2.06&Aring;' scene=''>

<table><tr><td colspan='2'>[[2nyr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2fzq 2fzq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NYR FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06&#8491;</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SVR:8,8-[CARBONYLBIS[IMINO-3,1-PHENYLENECARBONYLIMINO(4-METHYL-3,1-PHENYLENE)CARBONYLIMINO]]BIS-1,3,5-NAPHTHALENETRISULFONIC+ACID'>SVR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2nyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nyr OCA], [https://pdbe.org/2nyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nyr RCSB], [https://www.ebi.ac.uk/pdbsum/2nyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nyr ProSAT]</span></td></tr>

[https://www.uniprot.org/uniprot/SIR5_HUMAN SIR5_HUMAN] NAD-dependent lysine demalonylase and desuccinylase that specifically removes malonyl and succinyl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro.<ref>PMID:18680753</ref> <ref>PMID:21908771</ref> <ref>PMID:24140062</ref> <ref>PMID:22076378</ref>  

     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ny/2nyr_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nyr ConSurf].

*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Allali-Hassani A]]

[[Category: Antoshenko T]]

[[Category: Arrowsmith CH]]

[[Category: Bochkarev A]]

[[Category: Dong A]]

[[Category: Edwards AM]]

[[Category: Min JR]]

[[Category: Plotnikov AN]]

[[Category: Sundstrom M]]

[[Category: Weigelt J]]