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8bdb

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'''Unreleased structure'''
 
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The entry 8bdb is ON HOLD until Paper Publication
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==Ribulose-1,5-bisphosphate carboxylase/oxygenase from Griffithsia monilis==
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<StructureSection load='8bdb' size='340' side='right'caption='[[8bdb]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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Authors: Andersson, I., Gunn, L.H.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8bdb]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Griffithsia_monilis Griffithsia monilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BDB FirstGlance]. <br>
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Description: Ribulose-1,5-bisphosphate carboxylase/oxygenase from Griffithsia monilis
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HL2:(2S,3R)-2-AMINO-3-HYDROXY-4-METHYLPENTANOIC+ACID'>HL2</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bdb OCA], [https://pdbe.org/8bdb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bdb RCSB], [https://www.ebi.ac.uk/pdbsum/8bdb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bdb ProSAT]</span></td></tr>
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[[Category: Andersson, I]]
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</table>
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[[Category: Gunn, L.H]]
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== Function ==
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[https://www.uniprot.org/uniprot/A7UM67_GRIMO A7UM67_GRIMO] 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]
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__TOC__
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</StructureSection>
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[[Category: Griffithsia monilis]]
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[[Category: Large Structures]]
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[[Category: Andersson I]]
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[[Category: Gunn LH]]

Revision as of 08:15, 14 June 2023

Ribulose-1,5-bisphosphate carboxylase/oxygenase from Griffithsia monilis

PDB ID 8bdb

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