4lx9
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4lx9 is ON HOLD Authors: Liszczak, G.P., Marmorstein, R. Description: Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A== | |
| - | + | <StructureSection load='4lx9' size='340' side='right'caption='[[4lx9]], [[Resolution|resolution]] 1.98Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4lx9]] is a 1 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=4LX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LX9 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]] 1.98Å</td></tr> | |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</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=4lx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lx9 OCA], [https://pdbe.org/4lx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lx9 RCSB], [https://www.ebi.ac.uk/pdbsum/4lx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lx9 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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharolobus solfataricus P2]] | ||
| + | [[Category: Liszczak GP]] | ||
| + | [[Category: Marmorstein R]] | ||
Current revision
Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A
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