5KNK
Lipid A secondary acyltransferase LpxM from Acinetobacter baumannii with catalytic residue substitution (E127A)
Summary for 5KNK
Entry DOI | 10.2210/pdb5knk/pdb |
Related | 5KN7 |
Descriptor | Lipid A biosynthesis lauroyl acyltransferase, SULFATE ION, GLYCEROL, ... (6 entities in total) |
Functional Keywords | lpxm msbb waan, acyl transferase, lauryl transferase, transferase |
Biological source | Acinetobacter baumannii NIPH 410 |
Total number of polymer chains | 1 |
Total formula weight | 40001.64 |
Authors | Dovala, D.L.,Hu, Q.,Metzger IV, L.E. (deposition date: 2016-06-28, release date: 2016-09-28, Last modification date: 2023-09-27) |
Primary citation | Dovala, D.,Rath, C.M.,Hu, Q.,Sawyer, W.S.,Shia, S.,Elling, R.A.,Knapp, M.S.,Metzger, L.E. Structure-guided enzymology of the lipid A acyltransferase LpxM reveals a dual activity mechanism. Proc.Natl.Acad.Sci.USA, 113:E6064-E6071, 2016 Cited by PubMed: 27681620DOI: 10.1073/pnas.1610746113 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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