5FGN
Integral membrane protein lipooligosaccharide phosphoethanolamine transferase A (EptA) from Neisseria meningitidis
Summary for 5FGN
Entry DOI | 10.2210/pdb5fgn/pdb |
Related | 4KAV 4KAY |
Descriptor | lipooligosaccharide phosphoethanolamine transferase A, 2-O-octyl-beta-D-glucopyranose, DODECYL-BETA-D-MALTOSIDE, ... (5 entities in total) |
Functional Keywords | endotoxin biosynthesis, epta, membrane protein, phosphoethanolamine transferase, polymixin resistance, hydrolase, phosphotransferase, transferase |
Biological source | Neisseria meningitidis serogroup B |
Total number of polymer chains | 1 |
Total formula weight | 63160.66 |
Authors | Anandan, A.,Vrielink, A. (deposition date: 2015-12-21, release date: 2017-02-15, Last modification date: 2023-09-27) |
Primary citation | Anandan, A.,Evans, G.L.,Condic-Jurkic, K.,O'Mara, M.L.,John, C.M.,Phillips, N.J.,Jarvis, G.A.,Wills, S.S.,Stubbs, K.A.,Moraes, I.,Kahler, C.M.,Vrielink, A. Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding. Proc. Natl. Acad. Sci. U.S.A., 114:2218-2223, 2017 Cited by PubMed: 28193899DOI: 10.1073/pnas.1612927114 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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