This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5dy4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (22:05, 28 June 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of human Sirt2 in complex with a brominated 2nd generation SirReal inhibitor and NAD+==
==Crystal structure of human Sirt2 in complex with a brominated 2nd generation SirReal inhibitor and NAD+==
-
<StructureSection load='5dy4' size='340' side='right' caption='[[5dy4]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
+
<StructureSection load='5dy4' size='340' side='right'caption='[[5dy4]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5dy4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DY4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DY4 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5dy4]] 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=5DY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DY4 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5GN:N-{5-[(7-BROMONAPHTHALEN-1-YL)METHYL]-1,3-THIAZOL-2-YL}-2-[(4,6-DIMETHYLPYRIMIDIN-2-YL)SULFANYL]ACETAMIDE'>5GN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.77&#8491;</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=5dy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dy4 OCA], [http://pdbe.org/5dy4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dy4 RCSB], [http://www.ebi.ac.uk/pdbsum/5dy4 PDBsum]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GN:N-{5-[(7-BROMONAPHTHALEN-1-YL)METHYL]-1,3-THIAZOL-2-YL}-2-[(4,6-DIMETHYLPYRIMIDIN-2-YL)SULFANYL]ACETAMIDE'>5GN</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=5dy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dy4 OCA], [https://pdbe.org/5dy4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dy4 RCSB], [https://www.ebi.ac.uk/pdbsum/5dy4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dy4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://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>
+
[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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 17: Line 19:
</div>
</div>
<div class="pdbe-citations 5dy4" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5dy4" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Einsle, O]]
+
[[Category: Homo sapiens]]
-
[[Category: Gerhardt, S]]
+
[[Category: Large Structures]]
-
[[Category: Jung, M]]
+
[[Category: Einsle O]]
-
[[Category: Rumpf, T]]
+
[[Category: Gerhardt S]]
-
[[Category: Hydrolase]]
+
[[Category: Jung M]]
-
[[Category: Hydrolase inhibitor complex]]
+
[[Category: Rumpf T]]

Current revision

Crystal structure of human Sirt2 in complex with a brominated 2nd generation SirReal inhibitor and NAD+

PDB ID 5dy4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools