4b6c

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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=4b6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b6c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b6c RCSB], [http://www.ebi.ac.uk/pdbsum/4b6c 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=4b6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b6c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b6c RCSB], [http://www.ebi.ac.uk/pdbsum/4b6c PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/GYRB_MYCSM GYRB_MYCSM]] 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.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 12:24, 25 December 2014

Structure of the M. smegmatis GyrB ATPase domain in complex with an aminopyrazinamide

4b6c, resolution 2.20Å

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