4DMO
Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad
Summary for 4DMO
Entry DOI | 10.2210/pdb4dmo/pdb |
Descriptor | N-hydroxyarylamine O-acetyltransferase, 3-(1-methylpiperidinium-1-yl)propane-1-sulfonate (3 entities in total) |
Functional Keywords | acetyltransferase, transferase |
Biological source | Bacillus cereus |
Total number of polymer chains | 2 |
Total formula weight | 60863.97 |
Authors | Kubiak, X.,Li de la Sierra-Gallay, I.,Haouz, A.,Weber, P.,Rodrigues-Lima, F. (deposition date: 2012-02-08, release date: 2013-06-26, Last modification date: 2023-09-13) |
Primary citation | Kubiak, X.,Li de la Sierra-Gallay, I.,Chaffotte, A.F.,Pluvinage, B.,Weber, P.,Haouz, A.,Dupret, J.M.,Rodrigues-Lima, F. Structural and Biochemical Characterization of an Active Arylamine N-Acetyltransferase Possessing a Non-canonical Cys-His-Glu Catalytic Triad. J.Biol.Chem., 288:22493-22505, 2013 Cited by PubMed: 23770703DOI: 10.1074/jbc.M113.468595 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.14 Å) |
Structure validation
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