2w0w | pdb_00002w0w
From Proteopedia
CRYSTAL STRUCTURE OF GLMU FROM HAEMOPHILUS INFLUENZAE IN COMPLEX WITH QUINAZOLINE INHIBITOR 2
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Structural highlights
Function[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.[1] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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This page was last modified 21:38, 25 December 2014.