2yep

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==STRUCTURE OF AN N-TERMINAL NUCLEOPHILE (NTN) HYDROLASE, OAT2, IN COMPLEX WITH GLUTAMATE==
==STRUCTURE OF AN N-TERMINAL NUCLEOPHILE (NTN) HYDROLASE, OAT2, IN COMPLEX WITH GLUTAMATE==
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<StructureSection load='2yep' size='340' side='right' caption='[[2yep]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='2yep' size='340' side='right'caption='[[2yep]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2yep]] is a 8 chain structure with sequence from [http://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]. <br>
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<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>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene><br>
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</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>
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<tr><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>
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<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>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vzk|2vzk]], [[1vz8|1vz8]], [[2w4n|2w4n]], [[1vz6|1vz6]], [[1vz7|1vz7]], [[2v4i|2v4i]]</td></tr>
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<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>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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</table>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yep RCSB], [http://www.ebi.ac.uk/pdbsum/2yep PDBsum]</span></td></tr>
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== Function ==
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<table>
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[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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Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates.,Iqbal A, Clifton IJ, Chowdhury R, Ivison D, Domene C, Schofield CJ Org Biomol Chem. 2011 Sep 21;9(18):6219-25. Epub 2011 Jul 28. PMID:21796301<ref>PMID:21796301</ref>
Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates.,Iqbal A, Clifton IJ, Chowdhury R, Ivison D, Domene C, Schofield CJ Org Biomol Chem. 2011 Sep 21;9(18):6219-25. Epub 2011 Jul 28. PMID:21796301<ref>PMID:21796301</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2yep" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutamate N-acetyltransferase]]
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[[Category: Large Structures]]
[[Category: Streptomyces clavuligerus]]
[[Category: Streptomyces clavuligerus]]
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[[Category: Chowdhury, R.]]
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[[Category: Chowdhury R]]
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[[Category: Clifton, I J.]]
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[[Category: Clifton IJ]]
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[[Category: Iqbal, A.]]
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[[Category: Iqbal A]]
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[[Category: Schofield, C J.]]
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[[Category: Schofield CJ]]
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[[Category: Acyl enzyme]]
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[[Category: Acyltransferase]]
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[[Category: Hydrolase]]
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[[Category: Ntn hydrolase]]
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[[Category: Ornithine acetyl transferase]]
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[[Category: Transferase]]
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Current revision

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

PDB ID 2yep

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