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1ur5
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ur5' size='340' side='right' caption='[[1ur5]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='1ur5' size='340' side='right' caption='[[1ur5]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ur5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1ur5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29366 Atcc 29366]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UR5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UR5 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1guy|1guy]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1guy|1guy]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </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=1ur5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ur5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ur5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ur5 PDBsum]</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=1ur5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ur5 OCA], [http://pdbe.org/1ur5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ur5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ur5 PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/MDH_CHLAA MDH_CHLAA]] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 1ur5" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Atcc 29366]] |
[[Category: Malate dehydrogenase]] | [[Category: Malate dehydrogenase]] | ||
[[Category: Bjork, A]] | [[Category: Bjork, A]] | ||
Revision as of 13:30, 10 September 2015
STABILIZATION OF A TETRAMERIC MALATE DEHYDROGENASE BY INTRODUCTION OF A DISULFIDE BRIDGE AT THE DIMER/DIMER INTERFACE
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