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5c88
From Proteopedia
(Difference between revisions)
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<StructureSection load='5c88' size='340' side='right'caption='[[5c88]], [[Resolution|resolution]] 2.49Å' scene=''> | <StructureSection load='5c88' size='340' side='right'caption='[[5c88]], [[Resolution|resolution]] 2.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5c88]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5c88]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C88 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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=5c88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c88 OCA], [https://pdbe.org/5c88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c88 RCSB], [https://www.ebi.ac.uk/pdbsum/5c88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c88 ProSAT]</span></td></tr> | |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NAT_SACS2 NAT_SACS2] Displays alpha (N-terminal) acetyltransferase activity. Catalyzes the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein (PubMed:17511810, PubMed:23959863, PubMed:25728374). NAT is able to acetylate the alpha-amino group of methionine, alanine and serine N-terminal residue substrates, however it has a preference for Ser-N-terminal substrates (PubMed:17511810, PubMed:23959863, PubMed:25728374).<ref>PMID:17511810</ref> <ref>PMID:23959863</ref> <ref>PMID:25728374</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Saccharolobus solfataricus P2]] |
| - | + | [[Category: Chang YY]] | |
| - | [[Category: Chang | + | [[Category: Hsu CH]] |
| - | [[Category: Hsu | + | |
| - | + | ||
| - | + | ||
Revision as of 06:23, 7 June 2023
Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in monoclinic form
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