3nem: Difference between revisions
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==Aspartyl-tRNA synthetase complexed with aspartyl adenylate== | ==Aspartyl-tRNA synthetase complexed with aspartyl adenylate== | ||
<StructureSection load='3nem' size='340' side='right' caption='[[3nem]], [[Resolution|resolution]] 1.89Å' scene=''> | <StructureSection load='3nem' size='340' side='right'caption='[[3nem]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3nem]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3nem]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NEM 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]] 1.89Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMO:ASPARTYL-ADENOSINE-5-MONOPHOSPHATE'>AMO</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nem OCA], [https://pdbe.org/3nem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nem RCSB], [https://www.ebi.ac.uk/pdbsum/3nem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nem ProSAT]</span></td></tr> | ||
< | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SYD_THEKO SYD_THEKO] Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). Is specific for tRNA(Asp) since it aspartylates tRNA(Asn) 3 orders of magnitude less efficiently than tRNA(Asp).<ref>PMID:12149259</ref> <ref>PMID:12660169</ref> <ref>PMID:12730374</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Aminoacyl tRNA | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermococcus kodakarensis]] | ||
[[Category: Moras | [[Category: Moras D]] | ||
[[Category: Moulinier | [[Category: Moulinier L]] | ||
[[Category: Schmitt | [[Category: Schmitt E]] | ||