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3c0j

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==Structure of E. coli dihydrodipicolinate synthase complexed with hydroxypyruvate==
==Structure of E. coli dihydrodipicolinate synthase complexed with hydroxypyruvate==
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<StructureSection load='3c0j' size='340' side='right' caption='[[3c0j]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='3c0j' size='340' side='right'caption='[[3c0j]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3c0j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C0J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C0J FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3c0j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C0J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C0J 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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KYQ:(E)-N~6~-(1-CARBOXY-2-HYDROXYETHYLIDENE)-L-LYSINE'>KYQ</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KYQ:(E)-N~6~-(1-CARBOXY-2-HYDROXYETHYLIDENE)-L-LYSINE'>KYQ</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [https://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=3c0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c0j OCA], [http://pdbe.org/3c0j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c0j RCSB], [http://www.ebi.ac.uk/pdbsum/3c0j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c0j ProSAT]</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=3c0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c0j OCA], [https://pdbe.org/3c0j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c0j RCSB], [https://www.ebi.ac.uk/pdbsum/3c0j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c0j ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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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[[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</div>
</div>
<div class="pdbe-citations 3c0j" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3c0j" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
== References ==
== References ==
<references/>
<references/>
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[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
[[Category: Ecoli]]
[[Category: Ecoli]]
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[[Category: Large Structures]]
[[Category: Dobson, R C.J]]
[[Category: Dobson, R C.J]]
[[Category: Amino-acid biosynthesis]]
[[Category: Amino-acid biosynthesis]]

Revision as of 07:38, 27 January 2022

Structure of E. coli dihydrodipicolinate synthase complexed with hydroxypyruvate

PDB ID 3c0j

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