3vus

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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=3vus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vus OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vus RCSB], [http://www.ebi.ac.uk/pdbsum/3vus 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=3vus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vus OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vus RCSB], [http://www.ebi.ac.uk/pdbsum/3vus PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/PGAB_ECOLI PGAB_ECOLI]] Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PGA), a biofilm adhesin polysaccharide. N-deacetylation promotes PGA export through the PgaA porin.<ref>PMID:15090514</ref> <ref>PMID:18359807</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 18:57, 25 December 2014

Escherichia coli PgaB N-terminal domain

3vus, resolution 1.65Å

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