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: 18627129 DOI: 10.1021/bi800368y PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.3 Å)

Structure validation