5hao
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Structure function studies of R. palustris RubisCO (M331A mutant; CABP-bound)== | |
- | + | <StructureSection load='5hao' size='340' side='right' caption='[[5hao]], [[Resolution|resolution]] 2.18Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5hao]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HAO FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |
- | [[Category: | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5han|5han]], [[5hat|5hat]], [[5hjx|5hjx]], [[5hjy|5hjy]], [[5hk4|5hk4]], [[5hql|5hql]], [[5hqm|5hqm]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hao OCA], [http://pdbe.org/5hao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hao RCSB], [http://www.ebi.ac.uk/pdbsum/5hao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hao ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/RBL2_RHOPA RBL2_RHOPA]] 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 (By similarity). | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Ribulose-bisphosphate carboxylase]] | ||
+ | [[Category: Arbing, M A]] | ||
+ | [[Category: North, J A]] | ||
+ | [[Category: Satagopan, S]] | ||
+ | [[Category: Shin, A]] | ||
+ | [[Category: Tabita, F R]] | ||
+ | [[Category: Hexamer]] | ||
+ | [[Category: Lyase]] | ||
+ | [[Category: Rubisco]] |
Revision as of 16:45, 4 January 2017
Structure function studies of R. palustris RubisCO (M331A mutant; CABP-bound)
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