4kfg: 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=4kfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kfg RCSB], [http://www.ebi.ac.uk/pdbsum/4kfg 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=4kfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kfg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kfg RCSB], [http://www.ebi.ac.uk/pdbsum/4kfg PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/GYRB_ECOLI GYRB_ECOLI]] 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.<ref>PMID:12051843</ref> <ref>PMID:18642932</ref> <ref>PMID:20675723</ref> | |||
==See Also== | ==See Also== | ||
*[[Gyrase|Gyrase]] | *[[Gyrase|Gyrase]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 05:54, 25 December 2014
The DNA Gyrase B ATP binding domain of Escherichia coli in complex with a small molecule inhibitor.
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