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4rmf
From Proteopedia
(Difference between revisions)
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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=4rmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rmf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rmf RCSB], [http://www.ebi.ac.uk/pdbsum/4rmf PDBsum]</span></td></tr> | <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=4rmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rmf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rmf RCSB], [http://www.ebi.ac.uk/pdbsum/4rmf PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SYDND_MYCS2 SYDND_MYCS2]] Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).[HAMAP-Rule:MF_00044] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 18:01, 24 December 2014
Biochemical and structural characterization of mycobacterial aspartyl-tRNA synthetase AspS, a promising TB drug target
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