4mkv
From Proteopedia
(Difference between revisions)
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| - | + | ==Structure of Pisum sativum Rubisco with ABA== | |
| - | === | + | <StructureSection load='4mkv' size='340' side='right' caption='[[4mkv]], [[Resolution|resolution]] 2.15Å' scene=''> |
| - | + | == Structural highlights == | |
| - | ==Function== | + | <table><tr><td colspan='2'>[[4mkv]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MKV FirstGlance]. <br> |
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A8S:(2Z,4E)-5-[(1S)-1-HYDROXY-2,6,6-TRIMETHYL-4-OXOCYCLOHEX-2-EN-1-YL]-3-METHYLPENTA-2,4-DIENOIC+ACID'>A8S</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=RUB:RIBULOSE-1,5-DIPHOSPHATE'>RUB</scene></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='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=4mkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mkv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mkv RCSB], [http://www.ebi.ac.uk/pdbsum/4mkv PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/RBL_PEA RBL_PEA]] 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/RBS3_PEA RBS3_PEA]] 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). | [[http://www.uniprot.org/uniprot/RBL_PEA RBL_PEA]] 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/RBS3_PEA RBS3_PEA]] 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== |
| - | [[ | + | *[[RuBisCO|RuBisCO]] |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Pisum sativum]] | [[Category: Pisum sativum]] | ||
[[Category: Ribulose-bisphosphate carboxylase]] | [[Category: Ribulose-bisphosphate carboxylase]] | ||
| - | [[Category: Loewen, M C | + | [[Category: Loewen, M C]] |
| - | [[Category: Loewen, P C | + | [[Category: Loewen, P C]] |
| - | [[Category: Switala, J | + | [[Category: Switala, J]] |
[[Category: 5-bisphosphate]] | [[Category: 5-bisphosphate]] | ||
[[Category: Abscisic acid]] | [[Category: Abscisic acid]] | ||
Revision as of 07:41, 25 December 2014
Structure of Pisum sativum Rubisco with ABA
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