1aus

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (21:56, 26 March 2025) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 3: Line 3:
<StructureSection load='1aus' size='340' side='right'caption='[[1aus]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1aus' size='340' side='right'caption='[[1aus]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1aus]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUS FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1aus]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUS FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 2.2&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1aus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aus OCA], [http://pdbe.org/1aus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aus RCSB], [http://www.ebi.ac.uk/pdbsum/1aus PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aus ProSAT]</span></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=1aus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aus OCA], [https://pdbe.org/1aus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aus RCSB], [https://www.ebi.ac.uk/pdbsum/1aus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aus ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/RBL_SPIOL RBL_SPIOL]] 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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] [[http://www.uniprot.org/uniprot/RBS2_SPIOL RBS2_SPIOL]] 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.
+
[https://www.uniprot.org/uniprot/RBL_SPIOL RBL_SPIOL] 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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 15: Line 15:
<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1aus_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1aus_consurf.spt"</scriptWhenChecked>
-
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
Line 31: Line 31:
==See Also==
==See Also==
-
*[[RuBisCO|RuBisCO]]
+
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 37: Line 37:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Ribulose-bisphosphate carboxylase]]
 
[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
-
[[Category: Andersson, I]]
+
[[Category: Andersson I]]
-
[[Category: Taylor, T C]]
+
[[Category: Taylor TC]]

Current revision

ACTIVATED UNLIGANDED SPINACH RUBISCO

PDB ID 1aus

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools