5fda

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m (Protected "5fda" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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==The high resolution structure of apo form dihydrofolate reductase from Yersinia pestis at 1.55 A==
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<StructureSection load='5fda' size='340' side='right' caption='[[5fda]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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The entry 5fda is ON HOLD
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5fda]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FDA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FDA FirstGlance]. <br>
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Authors: Chang, C., Maltseva, N., Kim, Y., Makowska-Grzyska, M., Mulligan, R., Papazisi, L., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<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>
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Description: The high resolution structure of apo form dihydrofolate reductase from Yersinia pestis at 1.55 A
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<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>
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[[Category: Unreleased Structures]]
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<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=5fda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fda OCA], [http://pdbe.org/5fda PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fda RCSB], [http://www.ebi.ac.uk/pdbsum/5fda PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[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]
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__TOC__
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</StructureSection>
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[[Category: Dihydrofolate reductase]]
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[[Category: Anderson, W F]]
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[[Category: Structural genomic]]
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[[Category: Chang, C]]
[[Category: Joachimiak, A]]
[[Category: Joachimiak, A]]
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[[Category: Papazisi, L]]
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[[Category: Kim, Y]]
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[[Category: Mulligan, R]]
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[[Category: Makowska-Grzyska, M]]
[[Category: Makowska-Grzyska, M]]
[[Category: Maltseva, N]]
[[Category: Maltseva, N]]
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[[Category: Anderson, W.F]]
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[[Category: Mulligan, R]]
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[[Category: Center For Structural Genomics Of Infectious Diseases (Csgid)]]
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[[Category: Papazisi, L]]
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[[Category: Kim, Y]]
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[[Category: Csgid]]
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[[Category: Chang, C]]
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[[Category: Oxidoreductase]]
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[[Category: Yersinia pesti]]

Revision as of 19:41, 30 December 2015

The high resolution structure of apo form dihydrofolate reductase from Yersinia pestis at 1.55 A

5fda, resolution 1.55Å

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