2hne

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<StructureSection load='2hne' size='340' side='right'caption='[[2hne]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2hne' size='340' side='right'caption='[[2hne]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2hne]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Xance Xance]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HNE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2hne]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HNE 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=MG:MAGNESIUM+ION'>MG</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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yey|1yey]]</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=MG:MAGNESIUM+ION'>MG</scene></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/L-fuconate_dehydratase L-fuconate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.68 4.2.1.68] </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=2hne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hne OCA], [https://pdbe.org/2hne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hne RCSB], [https://www.ebi.ac.uk/pdbsum/2hne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hne ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2hne TOPSAN]</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=2hne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hne OCA], [http://pdbe.org/2hne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hne RCSB], [http://www.ebi.ac.uk/pdbsum/2hne PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hne ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2hne TOPSAN]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FUCD_XANCP FUCD_XANCP]] Plays a role in the catabolism of L-fucose. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion. L-fuconate is the preferred substrate with 15-fold lower activity observed for L-galactonate and 8-fold lower activity with D-arabinonate. No activity detected with D-fuconate. Can also catalyze the epimerization of L-talonate and D-ribonate, but at slow rates.<ref>PMID:17144652</ref>
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[https://www.uniprot.org/uniprot/FUCD_XANCP FUCD_XANCP] Plays a role in the catabolism of L-fucose. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion. L-fuconate is the preferred substrate with 15-fold lower activity observed for L-galactonate and 8-fold lower activity with D-arabinonate. No activity detected with D-fuconate. Can also catalyze the epimerization of L-talonate and D-ribonate, but at slow rates.<ref>PMID:17144652</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: L-fuconate dehydratase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Xance]]
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[[Category: Xanthomonas campestris pv. campestris]]
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[[Category: Almo, S C]]
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[[Category: Almo SC]]
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[[Category: Burley, S K]]
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[[Category: Burley SK]]
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[[Category: Fedorov, A A]]
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[[Category: Fedorov AA]]
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[[Category: Fedorov, E V]]
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[[Category: Fedorov EV]]
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[[Category: Gerlt, J A]]
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[[Category: Gerlt JA]]
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[[Category: Structural genomic]]
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[[Category: Yew WS]]
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[[Category: Yew, W S]]
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[[Category: Enolase superfamily]]
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[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Unknown function]]
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Current revision

Crystal structure of l-fuconate dehydratase from xanthomonas campestris pv. campestris str. ATCC 33913

PDB ID 2hne

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