1qah
From Proteopedia
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<StructureSection load='1qah' size='340' side='right'caption='[[1qah]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1qah' size='340' side='right'caption='[[1qah]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1qah]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1qah]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QAH FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qah OCA], [https://pdbe.org/1qah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qah RCSB], [https://www.ebi.ac.uk/pdbsum/1qah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qah ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/RIDA_RAT RIDA_RAT] 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.[UniProtKB:P52758] Also promotes endoribonucleolytic cleavage of some transcripts by promoting recruitment of the ribonuclease P/MRP complex (PubMed:10400702). Acts by bridging YTHDF2 and the ribonuclease P/MRP complex (By similarity). 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 (By similarity).[UniProtKB:P52758]<ref>PMID:10400702</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| - | [[Category: Carugo | + | [[Category: Djinovic Carugo K]] |
| - | [[Category: Oka | + | [[Category: Oka T]] |
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Current revision
CRYSTAL STRUCTURE OF PERCHLORIC ACID SOLUBLE PROTEIN-A TRANSLATIONAL INHIBITOR
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