4rmg: Difference between revisions

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New page: '''Unreleased structure''' The entry 4rmg is ON HOLD Authors: Rumpf, T., Schiedel, M., Karaman, B., Roessler, C., North, B.J., Lehotzky, A., Olah, J., Ladwein, K.I., Schmidtkunz, K., Ga...
 
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'''Unreleased structure'''


The entry 4rmg is ON HOLD
==Human Sirt2 in complex with SirReal2 and NAD+==
<StructureSection load='4rmg' size='340' side='right'caption='[[4rmg]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rmg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RMG 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]] 1.88&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3TE:2-[(4,6-DIMETHYLPYRIMIDIN-2-YL)SULFANYL]-N-[5-(NAPHTHALEN-1-YLMETHYL)-1,3-THIAZOL-2-YL]ACETAMIDE'>3TE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=4rmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rmg OCA], [https://pdbe.org/4rmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rmg RCSB], [https://www.ebi.ac.uk/pdbsum/4rmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rmg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SIR2_HUMAN SIR2_HUMAN] NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA.<ref>PMID:12620231</ref> <ref>PMID:12697818</ref> <ref>PMID:21081649</ref> <ref>PMID:21726808</ref>


Authors: Rumpf, T., Schiedel, M., Karaman, B., Roessler, C., North, B.J., Lehotzky, A., Olah, J., Ladwein, K.I., Schmidtkunz, K., Gajer, M., Pannek, M., Steegborn, C., Sinclair, D.A., Gerhardt, S., Ovadi, J., Schutkowski, M., Sippl, W., Einsle, O., Jung, M.
==See Also==
 
*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
Description: Human Sirt2 in complex with SirReal2 and NAD+
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Einsle O]]
[[Category: Gajer M]]
[[Category: Gerhardt S]]
[[Category: Jung M]]
[[Category: Karaman B]]
[[Category: Ladwein KI]]
[[Category: Lehotzky A]]
[[Category: North BJ]]
[[Category: Olah J]]
[[Category: Ovadi J]]
[[Category: Pannek M]]
[[Category: Roessler C]]
[[Category: Rumpf T]]
[[Category: Schiedel M]]
[[Category: Schmidtkunz K]]
[[Category: Schutkowski M]]
[[Category: Sinclair DA]]
[[Category: Sippl W]]
[[Category: Steegborn C]]
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