4J5H
Crystal Structure of B. thuringiensis AiiA mutant F107W with N-decanoyl-L-homoserine bound at the active site
Summary for 4J5H
Entry DOI | 10.2210/pdb4j5h/pdb |
Related | 4J5F |
Descriptor | N-acyl homoserine lactonase, ZINC ION, N-decanoyl-L-homoserine, ... (5 entities in total) |
Functional Keywords | aiia, lactonase, dizinc hydrolase, substrate specificity, quorum quenching, beta-hairpin loops, n-acyl homoserine lactone, hydrolase-hydrolase substrate complex, hydrolase/hydrolase substrate |
Biological source | Bacillus thuringiensis |
Total number of polymer chains | 1 |
Total formula weight | 29844.62 |
Authors | Liu, C.F.,Liu, D.,Momb, J.,Thomas, P.W.,Lajoie, A.,Petsko, G.A.,Fast, W.,Ringe, D. (deposition date: 2013-02-08, release date: 2013-06-26, Last modification date: 2024-02-28) |
Primary citation | Liu, C.F.,Liu, D.,Momb, J.,Thomas, P.W.,Lajoie, A.,Petsko, G.A.,Fast, W.,Ringe, D. A phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis. Biochemistry, 52:1603-1610, 2013 Cited by PubMed: 23387521DOI: 10.1021/bi400050j PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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