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3vpb

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<StructureSection load='3vpb' size='340' side='right'caption='[[3vpb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3vpb' size='340' side='right'caption='[[3vpb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vpb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulto Sulto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VPB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vpb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii_str._7 Sulfurisphaera tokodaii str. 7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VPB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vpc|3vpc]], [[3vpd|3vpd]]</div></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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">argE, STK_15050 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO]), lysW, STK_01925, STS023 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetylornithine_deacetylase Acetylornithine deacetylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.16 3.5.1.16] </span></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=3vpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpb OCA], [https://pdbe.org/3vpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vpb RCSB], [https://www.ebi.ac.uk/pdbsum/3vpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vpb 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=3vpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpb OCA], [https://pdbe.org/3vpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vpb RCSB], [https://www.ebi.ac.uk/pdbsum/3vpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vpb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ARGX_SULTO ARGX_SULTO]] Catalyzes the ATP-dependent formation of a covalent bond between the amino group of glutamate and the gamma-carboxyl group of the C-terminal glutamate residue in LysW (By similarity). [[https://www.uniprot.org/uniprot/LYSW_SULTO LYSW_SULTO]] Carrier protein that bears the covalently bound substrates for arginine and lysine biosynthesis; bound L-glutamate is sequentially converted to L-arginine, while bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine.
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[https://www.uniprot.org/uniprot/LYSW_SULTO LYSW_SULTO] Carrier protein that bears the covalently bound substrates for arginine and lysine biosynthesis; bound L-glutamate is sequentially converted to L-arginine, while bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine.
<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>
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[[Category: Acetylornithine deacetylase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sulto]]
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[[Category: Sulfurisphaera tokodaii str. 7]]
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[[Category: Kuzuyama, T]]
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[[Category: Kuzuyama T]]
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[[Category: Nishiyama, M]]
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[[Category: Nishiyama M]]
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[[Category: Ouchi, T]]
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[[Category: Ouchi T]]
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[[Category: Tomita, T]]
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[[Category: Tomita T]]
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[[Category: Atp-dependent amine/thiol ligase]]
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[[Category: Atp-dependent amine/thiol ligase family]]
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[[Category: Enzyme-carrier protein complex]]
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[[Category: Ligase]]
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[[Category: Lysw]]
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Revision as of 12:30, 8 November 2023

ArgX from Sulfolobus tokodaii complexed with LysW/Glu/ADP/Mg/Zn/Sulfate

PDB ID 3vpb

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