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5hi6
From Proteopedia
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| - | ''' | + | ==The high resolution structure of dihydrofolate reductase from Yersinia pestis complex with methotrxate as closed form== |
| - | + | <StructureSection load='5hi6' size='340' side='right' caption='[[5hi6]], [[Resolution|resolution]] 2.05Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5hi6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HI6 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MTX:METHOTREXATE'>MTX</scene></td></tr> | |
| - | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=5hi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hi6 OCA], [http://pdbe.org/5hi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hi6 RCSB], [http://www.ebi.ac.uk/pdbsum/5hi6 PDBsum]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A0A0B6NYF5_YERPE A0A0B6NYF5_YERPE]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.[PIRNR:PIRNR000194] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Dihydrofolate reductase]] | ||
| + | [[Category: Anderson, W F]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Chang, C]] | ||
[[Category: Joachimiak, A]] | [[Category: Joachimiak, A]] | ||
| - | [[Category: | + | [[Category: Kim, Y]] |
| - | + | ||
[[Category: Makowska-Grzyska, M]] | [[Category: Makowska-Grzyska, M]] | ||
[[Category: Maltseva, N]] | [[Category: Maltseva, N]] | ||
| - | [[Category: | + | [[Category: Mulligan, R]] |
| - | [[Category: | + | [[Category: Papazisi, L]] |
| - | [[Category: | + | [[Category: Csgid]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| + | [[Category: Yersinia pesti]] | ||
Revision as of 15:59, 3 February 2016
The high resolution structure of dihydrofolate reductase from Yersinia pestis complex with methotrxate as closed form
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