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3LNB

Crystal Structure Analysis of Arylamine N-acetyltransferase C from Bacillus anthracis

Summary for 3LNB
Entry DOI10.2210/pdb3lnb/pdb
DescriptorN-acetyltransferase family protein, COENZYME A, FORMIC ACID, ... (4 entities in total)
Functional Keywordsarylamine n-acetyltransferase, transferase, nat, acetyltransferase, acyltransferase
Biological sourceBacillus anthracis
Total number of polymer chains1
Total formula weight36162.07
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 citationPluvinage, 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: 22062153
DOI: 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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