3wqp
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==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 with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3WQP FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3wqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wqp OCA], [https://pdbe.org/3wqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wqp RCSB], [https://www.ebi.ac.uk/pdbsum/3wqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wqp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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> | ||
| - | + | ==See Also== | |
| - | + | *[[RuBisCO 3D structures|RuBisCO 3D structures]] | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermococcus kodakarensis KOD1]] | ||
| + | [[Category: Fujihashi M]] | ||
| + | [[Category: Kiriyama T]] | ||
| + | [[Category: Miki K]] | ||
| + | [[Category: Nishitani Y]] | ||
Current revision
Crystal structure of Rubisco T289D mutant from Thermococcus kodakarensis
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