5N6H
Structure of the membrane integral lipoprotein N-acyltransferase Lnt from E. coli
Summary for 5N6H
Entry DOI | 10.2210/pdb5n6h/pdb |
Descriptor | Apolipoprotein N-acyltransferase, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, GLYCEROL, ... (4 entities in total) |
Functional Keywords | membrane protein, lipoprotein, n-acyltransferase, lipidic cubic phase |
Biological source | Escherichia coli (strain K12) |
Total number of polymer chains | 2 |
Total formula weight | 126176.47 |
Authors | Huang, C.-Y.,Boland, C.,Howe, N.,Wiktor, M.,Vogeley, L.,Weichert, D.,Bailey, J.,Olieric, V.,Wang, M.,Caffrey, M. (deposition date: 2017-02-15, release date: 2017-07-12, Last modification date: 2024-05-08) |
Primary citation | Wiktor, M.,Weichert, D.,Howe, N.,Huang, C.Y.,Olieric, V.,Boland, C.,Bailey, J.,Vogeley, L.,Stansfeld, P.J.,Buddelmeijer, N.,Wang, M.,Caffrey, M. Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis. Nat Commun, 8:15952-15952, 2017 Cited by PubMed: 28675161DOI: 10.1038/ncomms15952 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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