4j15

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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=4j15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j15 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j15 RCSB], [http://www.ebi.ac.uk/pdbsum/4j15 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=4j15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j15 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j15 RCSB], [http://www.ebi.ac.uk/pdbsum/4j15 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/SYDC_HUMAN SYDC_HUMAN]] Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 21:48, 25 December 2014

Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex

4j15, resolution 2.24Å

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OCA

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