3wqp
From Proteopedia
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| - | ''' | + | ==Crystal structure of Rubisco T289D mutant from Thermococcus kodakarensis== |
| - | + | <StructureSection load='3wqp' size='340' side='right' caption='[[3wqp]], [[Resolution|resolution]] 2.25Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3wqp]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WQP FirstGlance]. <br> | |
| - | + | </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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1geh|1geh]], [[3a12|3a12]], [[3kdn|3kdn]], [[3kdo|3kdo]]</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> |
| - | [[Category: | + | <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=3wqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wqp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wqp RCSB], [http://www.ebi.ac.uk/pdbsum/3wqp PDBsum]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/RBL_THEKO RBL_THEKO]] Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase.[HAMAP-Rule:MF_01133]<ref>PMID:17303759</ref> <ref>PMID:20926376</ref> <ref>PMID:9988755</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ribulose-bisphosphate carboxylase]] | ||
[[Category: Fujihashi, M]] | [[Category: Fujihashi, M]] | ||
[[Category: Kiriyama, T]] | [[Category: Kiriyama, T]] | ||
| + | [[Category: Miki, K]] | ||
[[Category: Nishitani, Y]] | [[Category: Nishitani, Y]] | ||
| + | [[Category: Decamer]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Protein-ligand complex]] | ||
Revision as of 15:53, 7 February 2015
Crystal structure of Rubisco T289D mutant from Thermococcus kodakarensis
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