5hql

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Current revision (10:51, 16 August 2023) (edit) (undo)
 
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<StructureSection load='5hql' size='340' side='right'caption='[[5hql]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
<StructureSection load='5hql' size='340' side='right'caption='[[5hql]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5hql]] 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=5HQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HQL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5hql]] 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=5HQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HQL FirstGlance]. <br>
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</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>
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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]] 2.53&#8491;</td></tr>
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<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>
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<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=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<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]], [[5hqm|5hqm]]</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=5hql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hql OCA], [https://pdbe.org/5hql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hql RCSB], [https://www.ebi.ac.uk/pdbsum/5hql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hql ProSAT]</span></td></tr>
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<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>
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<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=5hql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hql OCA], [http://pdbe.org/5hql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hql RCSB], [http://www.ebi.ac.uk/pdbsum/5hql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hql ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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).
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[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==
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*[[RuBisCO|RuBisCO]]
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*[[RuBisCO 3D structures|RuBisCO 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Rhodobacillus palustris molisch 1907]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ribulose-bisphosphate carboxylase]]
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[[Category: Rhodopseudomonas palustris]]
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[[Category: Arbing, M A]]
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[[Category: Arbing MA]]
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[[Category: Cascio, D]]
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[[Category: Cascio D]]
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[[Category: North, J A]]
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[[Category: North JA]]
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[[Category: Satagopan, S]]
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[[Category: Satagopan S]]
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[[Category: Shin, A]]
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[[Category: Shin A]]
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[[Category: Tabita, F R]]
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[[Category: Tabita FR]]
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[[Category: Hexamer]]
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[[Category: Lyase]]
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[[Category: Rubisco]]
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Current revision

Structure function studies of R. palustris RubisCO (A47V-M331A mutant; CABP-bound; no expression tag)

PDB ID 5hql

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