5nv3: Difference between revisions

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 <SX load='5nv3' size='340' side='right' viewer='molstar' caption='[[5nv3]], [[Resolution|resolution]] 3.39&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5nv3]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NV3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NV3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5nv3]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NV3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.39&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbbL, cbbL1, rbcL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907]), cbbS, rbcS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907])</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=5nv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nv3 OCA], [https://pdbe.org/5nv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nv3 RCSB], [https://www.ebi.ac.uk/pdbsum/5nv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nv3 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/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nv3 OCA], [http://pdbe.org/5nv3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nv3 RCSB], [http://www.ebi.ac.uk/pdbsum/5nv3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nv3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RBL1_RHOSH RBL1_RHOSH]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]<ref>PMID:9882445</ref>  [[http://www.uniprot.org/uniprot/RBS1_RHOSH RBS1_RHOSH]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.<ref>PMID:9882445</ref>
+[https://www.uniprot.org/uniprot/RBL1_CERSP RBL1_CERSP] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]<ref>PMID:9882445</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 __TOC__
 </SX>
-[[Category: Rhodococcus capsulatus molisch 1907]]
+[[Category: Cereibacter sphaeroides]]
 [[Category: Large Structures]]
-[[Category: Ribulose-bisphosphate carboxylase]]
+[[Category: Bracher A]]
-[[Category: Bracher, A]]
+[[Category: Ciniawsky S]]
-[[Category: Ciniawsky, S]]
+[[Category: Hartl FU]]
-[[Category: Hartl, F U]]
+[[Category: Hayer-Hartl M]]
-[[Category: Hayer-Hartl, M]]
+[[Category: Milicic G]]
-[[Category: Milicic, G]]
+[[Category: Wendler P]]
-[[Category: Wendler, P]]
-[[Category: Beta barrel]]
-[[Category: Lyase]]