2c19: Difference between revisions

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-==5-(4-CARBOXY-2-OXO-BUTYLSULFANYL)-4-OXO-PENTANOIC ACID ACID BOUND TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA==
-<StructureSection load='2c19' size='340' side='right' caption='[[2c19]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
+==5-(4-Carboxy-2-oxo-butylsulfanyl)-4-oxo-pentanoic acid acid bound to Porphobilinogen synthase from Pseudomonas aeruginosa==
+<StructureSection load='2c19' size='340' side='right'caption='[[2c19]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2c19]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C19 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2c19]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C19 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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.05&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=C1X:(Z)-N~6~-[(4R,5S)-5-(2-CARBOXYETHYL)-4-(CARBOXYMETHYL)DIHYDRO-2H-THIOPYRAN-3(4H)-YLIDENE]-L-LYSINE'>C1X</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1X:(Z)-N~6~-[(4R,5S)-5-(2-CARBOXYETHYL)-4-(CARBOXYMETHYL)DIHYDRO-2H-THIOPYRAN-3(4H)-YLIDENE]-L-LYSINE'>C1X</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b4k|1b4k]], [[1gzg|1gzg]], [[1w54|1w54]], [[1w56|1w56]], [[1w5m|1w5m]], [[1w5n|1w5n]], [[1w5o|1w5o]], [[1w5p|1w5p]], [[1w5q|1w5q]], [[2c13|2c13]], [[2c14|2c14]], [[2c15|2c15]], [[2c18|2c18]]</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=2c19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c19 OCA], [https://pdbe.org/2c19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c19 RCSB], [https://www.ebi.ac.uk/pdbsum/2c19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c19 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] </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=2c19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c19 OCA], [http://pdbe.org/2c19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c19 RCSB], [http://www.ebi.ac.uk/pdbsum/2c19 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HEM2_PSEAE HEM2_PSEAE]] Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
+[https://www.uniprot.org/uniprot/HEM2_PSEAE HEM2_PSEAE] Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
 == 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/c1/2c19_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/2c19_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 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Porphobilinogen synthase]]
+[[Category: Large Structures]]
-[[Category: Frankenberg-Dinkel, N]]
+[[Category: Pseudomonas aeruginosa]]
-[[Category: Frere, F]]
+[[Category: Frankenberg-Dinkel N]]
-[[Category: Gacond, S]]
+[[Category: Frere F]]
-[[Category: Heinz, D W]]
+[[Category: Gacond S]]
-[[Category: Neier, R]]
+[[Category: Heinz DW]]
-[[Category: Nentwich, M]]
+[[Category: Neier R]]
-[[Category: Cocrystallization]]
+[[Category: Nentwich M]]
-[[Category: Enzyme mechanism]]
-[[Category: Lyase]]
-[[Category: Metalloenzyme]]
-[[Category: Porphyrin biosynthesis]]