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6FM9

Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1)

Summary for 6FM9
Entry DOI10.2210/pdb6fm9/pdb
DescriptorUDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase, (2S)-3-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-2-[(6E)-HEXADEC-6-ENOYLOXY]PROPYL (8E)-OCTADEC-8-ENOATE (2 entities in total)
Functional Keywordsprotein glycosylation, integral membrane protein, congenital myasthenic syndrome 13, structural genomics, structural genomics consortium, sgc, transferase
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight46962.79
Authors
Primary citationDong, Y.Y.,Wang, H.,Pike, A.C.W.,Cochrane, S.A.,Hamedzadeh, S.,Wyszynski, F.J.,Bushell, S.R.,Royer, S.F.,Widdick, D.A.,Sajid, A.,Boshoff, H.I.,Park, Y.,Lucas, R.,Liu, W.M.,Lee, S.S.,Machida, T.,Minall, L.,Mehmood, S.,Belaya, K.,Liu, W.W.,Chu, A.,Shrestha, L.,Mukhopadhyay, S.M.M.,Strain-Damerell, C.,Chalk, R.,Burgess-Brown, N.A.,Bibb, M.J.,Barry Iii, C.E.,Robinson, C.V.,Beeson, D.,Davis, B.G.,Carpenter, E.P.
Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance TB Antibiotic Design.
Cell, 175:1045-1058.e16, 2018
Cited by
PubMed: 30388443
DOI: 10.1016/j.cell.2018.10.037
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.6 Å)
Structure validation

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