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1rba

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{{Seed}}
 
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[[Image:1rba.png|left|200px]]
 
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==SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES==
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The line below this paragraph, containing "STRUCTURE_1rba", creates the "Structure Box" on the page.
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<StructureSection load='1rba' size='340' side='right'caption='[[1rba]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1rba]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RBA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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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=1rba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rba OCA], [https://pdbe.org/1rba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rba RCSB], [https://www.ebi.ac.uk/pdbsum/1rba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rba ProSAT]</span></td></tr>
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{{STRUCTURE_1rba| PDB=1rba | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RBL2_RHORU RBL2_RHORU] 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_01339]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rb/1rba_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rba ConSurf].
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<div style="clear:both"></div>
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===SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES===
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==See Also==
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*[[RuBisCO 3D structures|RuBisCO 3D structures]]
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__TOC__
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</StructureSection>
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The line below this paragraph, {{ABSTRACT_PUBMED_1606957}}, adds the Publication Abstract to the page
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[[Category: Large Structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 1606957 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1606957}}
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==About this Structure==
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1RBA is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RBA OCA].
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==Reference==
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<ref group="xtra">PMID:1606957</ref><references group="xtra"/>
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[[Category: Rhodospirillum rubrum]]
[[Category: Rhodospirillum rubrum]]
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[[Category: Ribulose-bisphosphate carboxylase]]
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[[Category: Schneider G]]
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[[Category: Schneider, G.]]
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[[Category: Soderlind E]]
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[[Category: Soderlind, E.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:04:50 2009''
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Current revision

SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES

PDB ID 1rba

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