5c88: Difference between revisions

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OCA

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 ==Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in monoclinic form==
-<StructureSection load='5c88' size='340' side='right' caption='[[5c88]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
+<StructureSection load='5c88' size='340' side='right'caption='[[5c88]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5c88]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C88 FirstGlance]. <br>
+<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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_alpha-N-acetyltransferase Peptide alpha-N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.88 2.3.1.88] </span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c88 OCA], [http://pdbe.org/5c88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c88 RCSB], [http://www.ebi.ac.uk/pdbsum/5c88 PDBsum]</span></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>
 </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;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Peptide alpha-N-acetyltransferase]]
+[[Category: Large Structures]]
-[[Category: Chang, Y Y]]
+[[Category: Saccharolobus solfataricus P2]]
-[[Category: Hsu, C H]]
+[[Category: Chang YY]]
-[[Category: Acetyltransferase]]
+[[Category: Hsu CH]]
-[[Category: Transferase]]