43cq: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry 43cq is ON HOLD~~

==Structure of wild type catalytic domains of E. coli threonine deaminase in complex with PLP==

~~Authors: Khodi, S.~~

== Structural highlights ==

<table><tr><td colspan='2'>[[43cq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=43CQ OCA]. For a guided tour on the structure components use [https://proteopedia.org/fgij/fg.htm?mol=43CQ FirstGlance].

~~Description:~~ Structure of wild type catalytic domains of E. coli threonine deaminase in complex with PLP

</td></tr><tr id='method'><td class="sblockLbl">[[Empirical_models|Method:]]</td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr>

[[Category: ~~Unreleased~~ Structures]]

<tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>

[[Category: Khodi, S]]

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[https://proteopedia.org/fgij/fg.htm?mol=43cq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=43cq OCA], [https://pdbe.org/43cq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=43cq RCSB], [https://www.ebi.ac.uk/pdbsum/43cq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=43cq ProSAT]</td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/ILVA_ECOLI ILVA_ECOLI] Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.<ref>PMID:13405870</ref>

== References ==

__TOC__

</StructureSection>

[[Category: Escherichia coli K-12]]

[[Category: Large Structures]]

[[Category: Khodi S]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 43cq is ON HOLD
+==Structure of wild type catalytic domains of E. coli threonine deaminase in complex with PLP==
+<StructureSection load='43cq' size='340' side='right'caption='[[43cq]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
-Authors: Khodi, S.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[43cq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=43CQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=43CQ FirstGlance]. <br>
-Description: Structure of wild type catalytic domains of E. coli threonine deaminase in complex with PLP
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
-[[Category: Khodi, S]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=43cq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=43cq OCA], [https://pdbe.org/43cq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=43cq RCSB], [https://www.ebi.ac.uk/pdbsum/43cq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=43cq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ILVA_ECOLI ILVA_ECOLI] Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.<ref>PMID:13405870</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Khodi S]]