3LNB
Crystal Structure Analysis of Arylamine N-acetyltransferase C from Bacillus anthracis
Summary for 3LNB
Entry DOI | 10.2210/pdb3lnb/pdb |
Descriptor | N-acetyltransferase family protein, COENZYME A, FORMIC ACID, ... (4 entities in total) |
Functional Keywords | arylamine n-acetyltransferase, transferase, nat, acetyltransferase, acyltransferase |
Biological source | Bacillus anthracis |
Total number of polymer chains | 1 |
Total formula weight | 36162.07 |
Authors | Li de la Sierra-Gallay, I.,Pluvinage, B.,Rodrigues-Lima, F. (deposition date: 2010-02-02, release date: 2011-01-26, Last modification date: 2023-11-01) |
Primary citation | Pluvinage, B.,Li de la Sierra-Gallay, I.,Kubiak, X.,Xu, X.,Dairou, J.,Dupret, J.M.,Rodrigues-Lima, F. The Bacillus anthracis arylamine N-acetyltransferase ((BACAN)NAT1) that inactivates sulfamethoxazole, reveals unusual structural features compared with the other NAT isoenzymes. Febs Lett., 585:3947-3952, 2011 Cited by PubMed: 22062153DOI: 10.1016/j.febslet.2011.10.041 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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