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3q0e

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Current revision (00:34, 28 December 2023) (edit) (undo)
 
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<StructureSection load='3q0e' size='340' side='right'caption='[[3q0e]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3q0e' size='340' side='right'caption='[[3q0e]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3q0e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q0E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q0E FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3q0e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q0E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q0E 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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;'>[[3q11|3q11]], [[3pzb|3pzb]], [[3pwk|3pwk]], [[3pyl|3pyl]], [[3pws|3pws]], [[3pzr|3pzr]], [[3pyx|3pyx]], [[3q1l|3q1l]]</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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VC_2036 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 "Bacillo virgola del Koch" Trevisan 1884])</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/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11] </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=3q0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q0e OCA], [https://pdbe.org/3q0e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q0e RCSB], [https://www.ebi.ac.uk/pdbsum/3q0e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q0e 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=3q0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q0e OCA], [https://pdbe.org/3q0e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q0e RCSB], [https://www.ebi.ac.uk/pdbsum/3q0e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q0e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DHAS1_VIBCH DHAS1_VIBCH]] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.<ref>PMID:12071715</ref>
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[https://www.uniprot.org/uniprot/DHAS1_VIBCH DHAS1_VIBCH] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.<ref>PMID:12071715</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>
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[[Category: Bacillo virgola del koch trevisan 1884]]
 
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[[Category: Aspartate-semialdehyde dehydrogenase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Liu, X]]
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[[Category: Vibrio cholerae]]
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[[Category: Pavlovsky, A G]]
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[[Category: Liu X]]
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[[Category: Viola, R E]]
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[[Category: Pavlovsky AG]]
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[[Category: Nadp]]
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[[Category: Viola RE]]
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[[Category: Oxidoreductase]]
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[[Category: Oxydoreductase]]
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Current revision

Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Vibrio Cholerae with product of S-allyl-L-cysteine sulfoxide

PDB ID 3q0e

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