5hqm
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure function studies of R. palustris RubisCO (R. palustris/R. rubrum chimera)== | |
| - | + | <StructureSection load='5hqm' size='340' side='right' caption='[[5hqm]], [[Resolution|resolution]] 1.95Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5hqm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HQM 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=K:POTASSIUM+ION'>K</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]], [[5hao|5hao]], [[5hat|5hat]], [[5hjx|5hjx]], [[5hjy|5hjy]], [[5hk4|5hk4]], [[5hql|5hql]]</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=5hqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hqm OCA], [http://pdbe.org/5hqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hqm RCSB], [http://www.ebi.ac.uk/pdbsum/5hqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hqm 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: Cascio, D]] | ||
| + | [[Category: Satagopan, S]] | ||
[[Category: Shin, A]] | [[Category: Shin, A]] | ||
| - | [[Category: Tabita, F | + | [[Category: Tabita, F R]] |
| - | [[Category: | + | [[Category: Hexamer]] |
| - | [[Category: | + | [[Category: Lyase]] |
| - | [[Category: | + | [[Category: Rubisco]] |
Revision as of 23:42, 25 January 2017
Structure function studies of R. palustris RubisCO (R. palustris/R. rubrum chimera)
| |||||||||||
