1tik

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CRYSTAL STRUCTURE OF ACYL CARRIER PROTEIN PHOSPHODIESTERASE

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 ==CRYSTAL STRUCTURE OF ACYL CARRIER PROTEIN PHOSPHODIESTERASE==
-<StructureSection load='1tik' size='340' side='right' caption='[[1tik]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='1tik' size='340' side='right'caption='[[1tik]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tik]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TIK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TIK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tik]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TIK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACPD, B1412 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1tik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tik OCA], [https://pdbe.org/1tik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tik RCSB], [https://www.ebi.ac.uk/pdbsum/1tik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tik ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1tik TOPSAN]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_phosphodiesterase [Acyl-carrier-protein] phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.14 3.1.4.14] </span></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=1tik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tik OCA], [http://pdbe.org/1tik PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tik RCSB], [http://www.ebi.ac.uk/pdbsum/1tik PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tik ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1tik TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AZOR_ECOLI AZOR_ECOLI]] Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. The enzyme can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes.<ref>PMID:2168383</ref>
+[https://www.uniprot.org/uniprot/AZOR_ECOLI AZOR_ECOLI] Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. The enzyme can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes.<ref>PMID:2168383</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ti/1tik_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 26: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Burley, S K]]
+[[Category: Large Structures]]
-[[Category: Kniewel, R]]
+[[Category: Burley SK]]
-[[Category: Lima, C D]]
+[[Category: Kniewel R]]
-[[Category: Structural genomic]]
+[[Category: Lima CD]]
-[[Category: Rajashankar, K R]]
+[[Category: Rajashankar KR]]
-[[Category: Solorzano, V]]
+[[Category: Solorzano V]]
-[[Category: Acpd]]
-[[Category: Hydrolase]]
-[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
-[[Category: PSI, Protein structure initiative]]
-[[Category: T1480]]

1tik

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CRYSTAL STRUCTURE OF ACYL CARRIER PROTEIN PHOSPHODIESTERASE

Structural highlights

Function

Evolutionary Conservation

References

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