3wqp
From Proteopedia
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==Crystal structure of Rubisco T289D mutant from Thermococcus kodakarensis== | ==Crystal structure of Rubisco T289D mutant from Thermococcus kodakarensis== | ||
| - | <StructureSection load='3wqp' size='340' side='right' caption='[[3wqp]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='3wqp' size='340' side='right'caption='[[3wqp]], [[Resolution|resolution]] 2.25Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3wqp]] is a 10 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3wqp]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain 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='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> | + | </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=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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1geh|1geh]], [[3a12|3a12]], [[3kdn|3kdn]], [[3kdo|3kdo]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rbcL, rbc, TK2290 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rbcL, rbc, TK2290 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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'>[ | + | <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> | </table> | ||
| - | {{Large structure}} | ||
== Function == | == 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> |
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| + | ==See Also== | ||
| + | *[[RuBisCO 3D structures|RuBisCO 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Ribulose-bisphosphate carboxylase]] | [[Category: Ribulose-bisphosphate carboxylase]] | ||
[[Category: Fujihashi, M]] | [[Category: Fujihashi, M]] | ||
Revision as of 05:46, 3 August 2022
Crystal structure of Rubisco T289D mutant from Thermococcus kodakarensis
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