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<StructureSection load='5hjy' size='340' side='right'caption='[[5hjy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='5hjy' size='340' side='right'caption='[[5hjy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5hjy]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodobacillus_palustris"_molisch_1907 "rhodobacillus palustris" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HJY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HJY FirstGlance]. <br>
<table><tr><td colspan='2'>[[5hjy]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HJY 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=CL:CHLORIDE+ION'>CL</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=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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]], [[5hk4|5hk4]], [[5hql|5hql]], [[5hqm|5hqm]]</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=5hjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hjy OCA], [https://pdbe.org/5hjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hjy RCSB], [https://www.ebi.ac.uk/pdbsum/5hjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hjy 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hjy OCA], [http://pdbe.org/5hjy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hjy RCSB], [http://www.ebi.ac.uk/pdbsum/5hjy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hjy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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).  
[https://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).


==See Also==
==See Also==
*[[RuBisCO|RuBisCO]]
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Rhodobacillus palustris molisch 1907]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ribulose-bisphosphate carboxylase]]
[[Category: Rhodopseudomonas palustris]]
[[Category: Arbing, M A]]
[[Category: Arbing MA]]
[[Category: Cascio, D]]
[[Category: Cascio D]]
[[Category: North, J A]]
[[Category: North JA]]
[[Category: Satagopan, S]]
[[Category: Satagopan S]]
[[Category: Shin, A]]
[[Category: Shin A]]
[[Category: Tabita, F R]]
[[Category: Tabita FR]]
[[Category: Hexamer]]
[[Category: Lyase]]
[[Category: Rubisco]]

Latest revision as of 07:39, 9 August 2023

Structure function studies of R. palustris RubisCO (I165T mutant; CABP-bound)

5hjy, resolution 2.30Å

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