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4r53

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==dihydrodipicolinate synthase from C. jejuni with vacant active site and vacant allosteric site==
==dihydrodipicolinate synthase from C. jejuni with vacant active site and vacant allosteric site==
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<StructureSection load='4r53' size='340' side='right' caption='[[4r53]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4r53' size='340' side='right'caption='[[4r53]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4r53]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Camje Camje]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R53 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R53 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4r53]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_subsp._jejuni_NCTC_11168_=_ATCC_700819 Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R53 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ly8|4ly8]], [[4m19|4m19]], [[4mlj|4mlj]], [[4mlr|4mlr]]</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=4r53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r53 OCA], [https://pdbe.org/4r53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r53 RCSB], [https://www.ebi.ac.uk/pdbsum/4r53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r53 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cj0806, dapA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192222 CAMJE])</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=4r53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r53 OCA], [http://pdbe.org/4r53 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r53 RCSB], [http://www.ebi.ac.uk/pdbsum/4r53 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r53 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DAPA_CAMJE DAPA_CAMJE]] 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_CAMJE DAPA_CAMJE] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4r53" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4r53" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
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[[Category: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]]
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[[Category: Camje]]
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[[Category: Large Structures]]
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[[Category: Conly, C J.T]]
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[[Category: Conly CJT]]
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[[Category: Aldolase]]
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[[Category: Lyase]]
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[[Category: Schiff-base]]
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[[Category: Tim barrel]]
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Revision as of 06:40, 2 March 2023

dihydrodipicolinate synthase from C. jejuni with vacant active site and vacant allosteric site

PDB ID 4r53

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