5hk4

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Current revision (07:39, 9 August 2023) (edit) (undo)
 
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<StructureSection load='5hk4' size='340' side='right'caption='[[5hk4]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='5hk4' size='340' side='right'caption='[[5hk4]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5hk4]] 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=5HK4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HK4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5hk4]] 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=5HK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HK4 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]] 2.15&#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]], [[5hql|5hql]], [[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=5hk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk4 OCA], [https://pdbe.org/5hk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hk4 RCSB], [https://www.ebi.ac.uk/pdbsum/5hk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hk4 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=5hk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk4 OCA], [http://pdbe.org/5hk4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hk4 RCSB], [http://www.ebi.ac.uk/pdbsum/5hk4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hk4 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)

PDB ID 5hk4

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