3wqp: Difference between revisions

Line 1:

'''~~Unreleased structure~~'''

==Crystal structure of Rubisco T289D mutant from Thermococcus kodakarensis==

~~The entry~~ 3wqp is ~~ON HOLD until Paper Publication~~

== 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 guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WQP FirstGlance].

~~Authors~~: ~~Fujihashi~~, M., ~~Nishitani~~, Y., ~~Kiriyama~~, T., ~~Miki~~, K.

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</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">[[Non-Standard_Residue|NonStd Res:]]</td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>

~~Description: Crystal structure of Rubisco T289D mutant from Thermococcus kodakarensis~~

[[~~Category~~: ~~Unreleased Structures~~]]

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

[[Category: ~~Miki, K~~]]

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[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]</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 ==

__TOC__

</StructureSection>

[[Category: Ribulose-bisphosphate carboxylase]]

[[Category: Fujihashi, M]]

[[Category: Kiriyama, T]]

[[Category: Miki, K]]

[[Category: Nishitani, Y]]

[[Category: Decamer]]

[[Category: Lyase]]

[[Category: Protein-ligand complex]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of Rubisco T289D mutant from Thermococcus kodakarensis==
+<StructureSection load='3wqp' size='340' side='right' caption='[[3wqp]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
-The entry 3wqp is ON HOLD  until Paper Publication
+== 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>
-Authors: Fujihashi, M., Nishitani, Y., Kiriyama, T., Miki, K.
+</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>
-Description: Crystal structure of Rubisco T289D mutant from Thermococcus kodakarensis
+<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>
-[[Category: Unreleased Structures]]
+<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: Miki, K]]
+<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: Kiriyama, T]]
+[[Category: Miki, K]]
 [[Category: Nishitani, Y]]
+[[Category: Decamer]]
+[[Category: Lyase]]
+[[Category: Protein-ligand complex]]