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3w0s

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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=3w0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w0s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w0s RCSB], [http://www.ebi.ac.uk/pdbsum/3w0s 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=3w0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w0s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w0s RCSB], [http://www.ebi.ac.uk/pdbsum/3w0s PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[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.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 22:46, 25 December 2014

Crystal structure of aminoglycoside phosphotransferase APH(4)-Ia, ternary complex with AMP-PNP and hygromycin B

3w0s, resolution 1.77Å

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