4k4o
From Proteopedia
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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=4k4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k4o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k4o RCSB], [http://www.ebi.ac.uk/pdbsum/4k4o 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=4k4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k4o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k4o RCSB], [http://www.ebi.ac.uk/pdbsum/4k4o PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/Q839Z1_ENTFA Q839Z1_ENTFA]] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings (By similarity).[HAMAP-Rule:MF_01898] | ||
==See Also== | ==See Also== | ||
Revision as of 20:45, 25 December 2014
The DNA Gyrase B ATP binding domain of Enterococcus faecalis in complex with a small molecule inhibitor
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