5t26

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Current revision (12:53, 4 October 2023) (edit) (undo)
 
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<StructureSection load='5t26' size='340' side='right'caption='[[5t26]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5t26' size='340' side='right'caption='[[5t26]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5t26]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco8a Eco8a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T26 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5t26]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_IAI1 Escherichia coli IAI1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T26 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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]] 2.1&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=74P:(E)-N~6~-(1-CARBOXY-3-OXOBUTYLIDENE)-L-LYSINE'>74P</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=74P:(E)-N~6~-(1-CARBOXY-3-OXOBUTYLIDENE)-L-LYSINE'>74P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5t25|5t25]]</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=5t26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t26 OCA], [https://pdbe.org/5t26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t26 RCSB], [https://www.ebi.ac.uk/pdbsum/5t26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t26 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapA, ECIAI1_2529 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585034 ECO8A])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5t26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t26 OCA], [http://pdbe.org/5t26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t26 RCSB], [http://www.ebi.ac.uk/pdbsum/5t26 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t26 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DAPA_ECO8A DAPA_ECO8A]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418]
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[https://www.uniprot.org/uniprot/DAPA_ECOLI DAPA_ECOLI] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:20503968</ref> <ref>PMID:8993314</ref>
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==See Also==
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*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
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[[Category: Escherichia coli IAI1]]
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[[Category: Eco8a]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chooback, L]]
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[[Category: Chooback L]]
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[[Category: Fleming, C D]]
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[[Category: Fleming CD]]
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[[Category: Karsten, W E]]
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[[Category: Karsten WE]]
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[[Category: Seabourn, P]]
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[[Category: Seabourn P]]
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[[Category: Thomas, L M]]
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[[Category: Thomas LM]]
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[[Category: Acetopyruvate modification]]
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[[Category: Dihydrodipicolinate synthase]]
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[[Category: Kinetic]]
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[[Category: Lyase]]
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Current revision

Kinetic, Spectral and Structural Characterization of the Slow Binding Inhibitor Acetopyruvate with Dihydrodipicolinate Synthase from Escherichia coli.

PDB ID 5t26

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OCA

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