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3w0m
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(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=3w0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w0m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w0m RCSB], [http://www.ebi.ac.uk/pdbsum/3w0m 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=3w0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w0m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w0m RCSB], [http://www.ebi.ac.uk/pdbsum/3w0m PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/KHYB_ECOLX KHYB_ECOLX]] The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation. Only phosphorylates hygromycin and closely related compounds such as demethyl analogs and destomycin. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 22:37, 24 December 2014
Crystal structure of a thermostable mutant of aminoglycoside phosphotransferase APH(4)-Ia, apo form
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