3d4b
From Proteopedia
(Difference between revisions)
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==Crystal structure of Sir2Tm in complex with Acetyl p53 peptide and DADMe-NAD+== | ==Crystal structure of Sir2Tm in complex with Acetyl p53 peptide and DADMe-NAD+== | ||
- | <StructureSection load='3d4b' size='340' side='right' caption='[[3d4b]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='3d4b' size='340' side='right'caption='[[3d4b]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3d4b]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3d4b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D4B FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DZD:5-O-[(R)-{[(R)-{[(3R,4R)-1-(3-CARBAMOYLBENZYL)-4-HYDROXYPYRROLIDIN-3-YL]METHOXY}(HYDROXY)PHOSPHORYL]METHYL}(HYDROXY)PHOSPHORYL]ADENOSINE'>DZD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DZD:5-O-[(R)-{[(R)-{[(3R,4R)-1-(3-CARBAMOYLBENZYL)-4-HYDROXYPYRROLIDIN-3-YL]METHOXY}(HYDROXY)PHOSPHORYL]METHYL}(HYDROXY)PHOSPHORYL]ADENOSINE'>DZD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr> | ||
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">npdA, TM_0490 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">npdA, TM_0490 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d4b OCA], [https://pdbe.org/3d4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d4b RCSB], [https://www.ebi.ac.uk/pdbsum/3d4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d4b ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/NPD_THEMA NPD_THEMA]] NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. Has also depropionylation activity in vitro. Also able to ADP-ribosylate peptide substrates with Arg or Lys in the +2 position. The role of this function in vivo is not clear.<ref>PMID:17684016</ref> <ref>PMID:16905097</ref> <ref>PMID:19801667</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 43589]] | [[Category: Atcc 43589]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Daines, A]] | [[Category: Daines, A]] | ||
[[Category: Fatkins, D]] | [[Category: Fatkins, D]] |
Revision as of 07:53, 2 February 2022
Crystal structure of Sir2Tm in complex with Acetyl p53 peptide and DADMe-NAD+
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Categories: Atcc 43589 | Large Structures | Daines, A | Fatkins, D | Hawse, W F | Hoff, K G | Schramm, V L | Wolberger, C | Zheng, W | Zubkova, O V | Cytoplasm | Hydrolase | Metal-binding | Nad | Rossmann fold | Zinc