1hw2: Difference between revisions

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<StructureSection load='1hw2' size='340' side='right'caption='[[1hw2]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
<StructureSection load='1hw2' size='340' side='right'caption='[[1hw2]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1hw2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HW2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1hw2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HW2 FirstGlance]. <br>
</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>
</td></tr><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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hw1|1hw1]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hw1|1hw1]]</div></td></tr>
<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=1hw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hw2 OCA], [http://pdbe.org/1hw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1hw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hw2 ProSAT]</span></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=1hw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hw2 OCA], [https://pdbe.org/1hw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hw2 RCSB], [https://www.ebi.ac.uk/pdbsum/1hw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hw2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/FADR_ECOLI FADR_ECOLI]] Multifunctional regulator of fatty acid metabolism. Represses transcription of at least eight genes required for fatty acid transport and beta-oxidation including fadA, fadB, fadD, fadL and fadE. Activates transcription of at least three genes required for unsaturated fatty acid biosynthesis: fabA, fabB and iclR, the gene encoding the transcriptional regulator of the aceBAK operon encoding the glyoxylate shunt enzymes. Binding of FadR is specifically inhibited by long chain fatty acyl-CoA compounds.  
[[https://www.uniprot.org/uniprot/FADR_ECOLI FADR_ECOLI]] Multifunctional regulator of fatty acid metabolism. Represses transcription of at least eight genes required for fatty acid transport and beta-oxidation including fadA, fadB, fadD, fadL and fadE. Activates transcription of at least three genes required for unsaturated fatty acid biosynthesis: fabA, fabB and iclR, the gene encoding the transcriptional regulator of the aceBAK operon encoding the glyoxylate shunt enzymes. Binding of FadR is specifically inhibited by long chain fatty acyl-CoA compounds.  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

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