4knx

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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=4knx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4knx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4knx RCSB], [http://www.ebi.ac.uk/pdbsum/4knx 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=4knx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4knx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4knx RCSB], [http://www.ebi.ac.uk/pdbsum/4knx PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/GLMU_HAEIN GLMU_HAEIN]] Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.<ref>PMID:18029420</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 03:22, 25 December 2014

Hin GlmU Bound to WG176

4knx, resolution 1.90Å

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