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<StructureSection load='2yep' size='340' side='right'caption='[[2yep]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='2yep' size='340' side='right'caption='[[2yep]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2yep]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/As_4.1611 As 4.1611]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2w4n 2w4n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YEP FirstGlance]. <br>
<table><tr><td colspan='2'>[[2yep]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2w4n 2w4n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YEP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</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]] 2.7&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TH5:O-ACETYL-L-THREONINE'>TH5</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=TH5:O-ACETYL-L-THREONINE'>TH5</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vzk|2vzk]], [[1vz8|1vz8]], [[2w4n|2w4n]], [[1vz6|1vz6]], [[1vz7|1vz7]], [[2v4i|2v4i]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate_N-acetyltransferase Glutamate N-acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.35 2.3.1.35] </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=2yep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yep OCA], [https://pdbe.org/2yep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yep RCSB], [https://www.ebi.ac.uk/pdbsum/2yep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yep ProSAT]</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=2yep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yep OCA], [https://pdbe.org/2yep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yep RCSB], [https://www.ebi.ac.uk/pdbsum/2yep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yep ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GNAT2_STRCL GNAT2_STRCL]] Catalyzes the biosynthesis of ornithine by transacetylation between N(2)-acetylornithine and glutamate. It can also use L-arginine, L-glutamine and L-lysine as acetyl acceptors.<ref>PMID:11985581</ref>
[https://www.uniprot.org/uniprot/GNAT2_STRCL GNAT2_STRCL] Catalyzes the biosynthesis of ornithine by transacetylation between N(2)-acetylornithine and glutamate. It can also use L-arginine, L-glutamine and L-lysine as acetyl acceptors.<ref>PMID:11985581</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: As 4 1611]]
[[Category: Glutamate N-acetyltransferase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chowdhury, R]]
[[Category: Streptomyces clavuligerus]]
[[Category: Clifton, I J]]
[[Category: Chowdhury R]]
[[Category: Iqbal, A]]
[[Category: Clifton IJ]]
[[Category: Schofield, C J]]
[[Category: Iqbal A]]
[[Category: Acyl enzyme]]
[[Category: Schofield CJ]]
[[Category: Acyltransferase]]
[[Category: Hydrolase]]
[[Category: Ntn hydrolase]]
[[Category: Ornithine acetyl transferase]]
[[Category: Transferase]]

Latest revision as of 08:13, 23 August 2023

STRUCTURE OF AN N-TERMINAL NUCLEOPHILE (NTN) HYDROLASE, OAT2, IN COMPLEX WITH GLUTAMATE

2yep, resolution 2.70Å

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