5VRH
Apolipoprotein N-acyltransferase C387S active site mutant
Summary for 5VRH
Entry DOI | 10.2210/pdb5vrh/pdb |
Related | 5VRG |
Descriptor | Apolipoprotein N-acyltransferase, (2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, MAGNESIUM ION, ... (7 entities in total) |
Functional Keywords | lnt c387s, acyl transferase, membrane protein, transferase |
Biological source | Escherichia coli (strain K12) |
Cellular location | Cell inner membrane ; Multi- pass membrane protein : P23930 |
Total number of polymer chains | 1 |
Total formula weight | 60185.21 |
Authors | Murray, J.M.,Noland, C.L. (deposition date: 2017-05-10, release date: 2017-07-12, Last modification date: 2023-10-04) |
Primary citation | Noland, C.L.,Kattke, M.D.,Diao, J.,Gloor, S.L.,Pantua, H.,Reichelt, M.,Katakam, A.K.,Yan, D.,Kang, J.,Zilberleyb, I.,Xu, M.,Kapadia, S.B.,Murray, J.M. Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase. Proc. Natl. Acad. Sci. U.S.A., 114:E6044-E6053, 2017 Cited by PubMed: 28698362DOI: 10.1073/pnas.1707813114 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.137 Å) |
Structure validation
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