1ir1: Difference between revisions

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<StructureSection load='1ir1' size='340' side='right'caption='[[1ir1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1ir1' size='340' side='right'caption='[[1ir1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ir1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Spiol Spiol]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bur 1bur]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IR1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ir1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bur 1bur]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IR1 FirstGlance]. <br>
</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=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]] 1.8&#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>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</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=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ir2|1ir2]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=1ir1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ir1 OCA], [https://pdbe.org/1ir1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ir1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ir1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ir1 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=1ir1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ir1 OCA], [https://pdbe.org/1ir1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ir1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ir1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ir1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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] [[https://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]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ribulose-bisphosphate carboxylase]]
[[Category: Spinacia oleracea]]
[[Category: Spiol]]
[[Category: Inoue T]]
[[Category: Inoue, T]]
[[Category: Kai Y]]
[[Category: Kai, Y]]
[[Category: Kato K]]
[[Category: Kato, K]]
[[Category: Kumei M]]
[[Category: Kumei, M]]
[[Category: Matsumura H]]
[[Category: Matsumura, H]]
[[Category: Mizohata E]]
[[Category: Mizohata, E]]
[[Category: Okano Y]]
[[Category: Okano, Y]]
[[Category: Onodera J]]
[[Category: Onodera, J]]
[[Category: Shibata N]]
[[Category: Shibata, N]]
[[Category: Takuma H]]
[[Category: Takuma, H]]
[[Category: Yokota A]]
[[Category: Yokota, A]]
[[Category: Alpha/beta barrel]]
[[Category: Lyase]]