3fkr: Difference between revisions
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==Structure of L-2-keto-3-deoxyarabonate dehydratase complex with pyruvate== | |||
<StructureSection load='3fkr' size='340' side='right'caption='[[3fkr]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3fkr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_29145 Atcc 29145]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FKR FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fkk|3fkk]]</div></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fkr OCA], [https://pdbe.org/3fkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fkr RCSB], [https://www.ebi.ac.uk/pdbsum/3fkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fkr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/KDADA_AZOBR KDADA_AZOBR]] Catalyzes the dehydration of L-2-keto-3-deoxyarabonate (L-KDA) to alpha-ketoglutaric semialdehyde (alphaKGSA). Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source.<ref>PMID:16950779</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fk/3fkr_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fkr ConSurf]. | |||
<div style="clear:both"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Atcc 29145]] | |||
[[Category: Large Structures]] | |||
[[Category: Mikami, B]] | |||
[[Category: Shimada, N]] | |||
[[Category: Complex]] | |||
[[Category: Dhdps/nal family]] | |||
[[Category: Lyase]] | |||
[[Category: Pyruvate]] |