3DHC
1.3 Angstrom Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homocysteine Bound to The catalytic Metal Center
Summary for 3DHC
Entry DOI | 10.2210/pdb3dhc/pdb |
Related | 2A7M 2R2D 3DHA 3DHB |
Descriptor | N-Acyl Homoserine Lactone Hydrolase, ZINC ION, N-hexanoyl-L-homocysteine, ... (5 entities in total) |
Functional Keywords | zinc bimetallohydrolase, qourum quenching, n-acyl homocysteine thiolactone, product complex, ahl lactonase, general acid, catalytic mechanism, hydrolase |
Biological source | Bacillus thuringiensis serovar kurstaki |
Total number of polymer chains | 1 |
Total formula weight | 29581.35 |
Authors | Liu, D.,Momb, J.,Thomas, P.W.,Moulin, A.,Petsko, G.A.,Fast, W.,Ringe, D. (deposition date: 2008-06-17, release date: 2008-07-29, Last modification date: 2023-08-30) |
Primary citation | Liu, D.,Momb, J.,Thomas, P.W.,Moulin, A.,Petsko, G.A.,Fast, W.,Ringe, D. Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures. Biochemistry, 47:7706-7714, 2008 Cited by PubMed: 18627129DOI: 10.1021/bi800368y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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