5oc5

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m (Protected "5oc5" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5oc5 is ON HOLD until Paper Publication
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==Crystal structure of human tRNA-dihydrouridine(20) synthase dsRBD K419A-K420A mutant==
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<StructureSection load='5oc5' size='340' side='right' caption='[[5oc5]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5oc5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OC5 FirstGlance]. <br>
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Description:
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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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5oc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oc5 OCA], [http://pdbe.org/5oc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oc5 RCSB], [http://www.ebi.ac.uk/pdbsum/5oc5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oc5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/DUS2L_HUMAN DUS2L_HUMAN]] Dihydrouridine synthase. Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Negatively regulates the activation of EIF2AK2/PKR.<ref>PMID:15994936</ref> <ref>PMID:18096616</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bou-nader, C]]
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[[Category: Hamdane, D]]
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[[Category: Pecqueur, L]]
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[[Category: Double-stranded rna-binding domain]]
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[[Category: Rna binding protein]]

Revision as of 08:10, 26 December 2018

Crystal structure of human tRNA-dihydrouridine(20) synthase dsRBD K419A-K420A mutant

5oc5, resolution 1.89Å

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