Human GPT (DPAGT1) H129 variant in complex with tunicamycin

(1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate
1-Palmitoyl-2-Oleoyl-sn-Glycero-3-[Phospho-(1-glycerol)]; PHOSPHATIDYLGLYCEROL

GlcNAc-1-P-transferase-tunicamycin complex structure reveals basis for inhibition of N-glycosylation.

UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase

GlcNAc-1-P transferase,GPT,N-acetylglucosamine-1-phosphate transferase

MWAFSELPMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLNKTSRQQIPESQGVISGAVFLIILFCFIPFPFLN
CFVKEQCKAFPHHEFVALIGALLAICCMIFLGFADDVLNLRWRHKLLLHTAASLPLLMVYFTNFGNTTIVVPKPFRPILG
LHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSLYFMIPFFFTTLGLLY
HNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPRLNIKTGKLEMSYSK
FKTKSLSFLGTFILKVAESLQLVTVHQSETEDGEFTECNNMTLINLLLKVLGPIHERNLTLLLLLLQILGSAITFSIRYQ
LVRLFYDVTNSLEVLFQ

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)

N-linked glycosylation, endoplasmic reticulum, tunicamycin, natural product, TRANSFERASE, TRANSFERASE-ANTIBIOTIC complex

MWAFSELPMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLNKTSRQQIPESQGVISGAVFLIILFCFIPFPFLN
CFVKEQCKAFPHHEFVALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPKPFRPILG
LHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSLYFMIPFFFTTLGLLY
HNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPRLNIKTGKLEMSYSK
FKTKSLSFLGTFILKVAESLQLVTVHQSETEDGEFTECNNMTLINLLLKVLGPIHERNLTLLLLLLQILGSAITFSIRYQ
LVRLFYDV