1oni
From Proteopedia
(Difference between revisions)
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<StructureSection load='1oni' size='340' side='right'caption='[[1oni]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1oni' size='340' side='right'caption='[[1oni]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1oni]] is a 9 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1oni]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ONI FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oni OCA], [https://pdbe.org/1oni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oni RCSB], [https://www.ebi.ac.uk/pdbsum/1oni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oni ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/RIDA_HUMAN RIDA_HUMAN] Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase.<ref>PMID:20817725</ref> <ref>PMID:22094463</ref> Also promotes endoribonucleolytic cleavage of some transcripts by promoting recruitment of the ribonuclease P/MRP complex (PubMed:8973653, PubMed:30930054). Acts by bridging YTHDF2 and the ribonuclease P/MRP complex (PubMed:30930054). RIDA/HRSP12 binds to N6-methyladenosine (m6A)-containing mRNAs containing a 5'-GGUUC-3' motif: cooperative binding of RIDA/HRSP12 and YTHDF2 to such transcripts lead to recruitment of the ribonuclease P/MRP complex and subsequent endoribonucleolytic cleavage (PubMed:30930054).<ref>PMID:30930054</ref> <ref>PMID:8973653</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oni ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oni ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Delbrueck | + | [[Category: Delbrueck H]] |
| - | [[Category: Erdmann | + | [[Category: Erdmann MF]] |
| - | [[Category: Heinemann | + | [[Category: Heinemann U]] |
| - | [[Category: Manjasetty | + | [[Category: Manjasetty BA]] |
| - | [[Category: Mueller | + | [[Category: Mueller U]] |
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Current revision
Crystal structure of a human p14.5, a translational inhibitor reveals different mode of ligand binding near the invariant residues of the Yjgf/UK114 protein family
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