2vdh: Difference between revisions

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 <StructureSection load='2vdh' size='340' side='right'caption='[[2vdh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vdh]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VDH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vdh]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VDH 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=EDO:1,2-ETHANEDIOL'>EDO</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">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=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</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;'>[[1uw9|1uw9]], [[1uzh|1uzh]], [[2v68|2v68]], [[2v69|2v69]], [[1gk8|1gk8]], [[1ir2|1ir2]], [[1uwa|1uwa]], [[1uzd|1uzd]], [[2v63|2v63]], [[2v67|2v67]], [[2v6a|2v6a]], [[2vdi|2vdi]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2vdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdh OCA], [https://pdbe.org/2vdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vdh RCSB], [https://www.ebi.ac.uk/pdbsum/2vdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vdh ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/RBL_CHLRE RBL_CHLRE]] 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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] [[https://www.uniprot.org/uniprot/RBS1_CHLRE RBS1_CHLRE]] 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.
+[https://www.uniprot.org/uniprot/RBL_CHLRE RBL_CHLRE] 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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 __TOC__
 </StructureSection>
-[[Category: Chlre]]
+[[Category: Chlamydomonas reinhardtii]]
 [[Category: Large Structures]]
-[[Category: Ribulose-bisphosphate carboxylase]]
+[[Category: Andersson I]]
-[[Category: Andersson, I]]
+[[Category: Garcia-Murria M-J]]
-[[Category: Garcia-Murria, M J]]
+[[Category: Karkehabadi S]]
-[[Category: Karkehabadi, S]]
+[[Category: Marin-Navarro J]]
-[[Category: Marin-Navarro, J]]
+[[Category: Moreno J]]
-[[Category: Moreno, J]]
+[[Category: Satagopan S]]
-[[Category: Satagopan, S]]
+[[Category: Spreitzer RJ]]
-[[Category: Spreitzer, R J]]
-[[Category: Acetylation]]
-[[Category: Calvin cycle]]
-[[Category: Carbon dioxide fixation]]
-[[Category: Chloroplast]]
-[[Category: Co2/o2 specificity]]
-[[Category: Hydroxylation]]
-[[Category: Lyase]]
-[[Category: Magnesium]]
-[[Category: Metal-binding]]
-[[Category: Methylation]]
-[[Category: Monooxygenase]]
-[[Category: Oxidoreductase]]
-[[Category: Photorespiration]]
-[[Category: Photosynthesis]]
-[[Category: Plastid]]
-[[Category: Rubisco]]
-[[Category: Transit peptide]]
-[[Category: Vicinal cysteine]]