8AQ4
In surfo structure of the membrane integral lipoprotein N-acyltransferase Lnt from E. coli in complex with TITC and lyso-PE
Summary for 8AQ4
Entry DOI | 10.2210/pdb8aq4/pdb |
Descriptor | Apolipoprotein N-acyltransferase, CHLORIDE ION, 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE, ... (11 entities in total) |
Functional Keywords | lnt, apolipoprotein n-acyltransferase, bacterial lipoproteins., transferase |
Biological source | Escherichia coli K-12 |
Total number of polymer chains | 1 |
Total formula weight | 64993.94 |
Authors | Huang, C.-Y.,Weichert, D.,Boland, C.,Smithers, L.,Olieric, V.,Wang, M.,Caffrey, M. (deposition date: 2022-08-11, release date: 2023-07-12, Last modification date: 2024-02-07) |
Primary citation | Smithers, L.,Degtjarik, O.,Weichert, D.,Huang, C.Y.,Boland, C.,Bowen, K.,Oluwole, A.,Lutomski, C.,Robinson, C.V.,Scanlan, E.M.,Wang, M.,Olieric, V.,Shalev-Benami, M.,Caffrey, M. Structure snapshots reveal the mechanism of a bacterial membrane lipoprotein N -acyltransferase. Sci Adv, 9:eadf5799-eadf5799, 2023 Cited by PubMed: 37390210DOI: 10.1126/sciadv.adf5799 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.62 Å) |
Structure validation
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