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Ligands
Code Name Style Show Link
CYK N-hexanoyl-L-homocysteine
GOL Glycerol
ZN Zinc ion
Non-standard Residues
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Glycosylation
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Code : 3DHC   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : 1.3 Angstrom Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homocysteine Bound to The catalytic Metal Center
Release Data : 2008-07-29
Compound :
mol_id molecule chains synonym
1 N-Acyl Homoserine Lactone Hydrolase A AiiA-like protein
ec: 3.1.1.-
Source :
mol_id organism_scientific expression_system
1 Bacillus thuringiensis serovar kurstaki  (taxid:29339) Escherichia coli
gene: aiiA
expression_system_strain: BL21(DE3)
expression_system_vector_type: Plasmid
expression_system_plasmid: pMAL
other_details: TEV protease was used to cut off the fusion protein MBP resulting in 4 extra residues at the N terminus. The extra residues are not observed in the structure
Authors : Liu, D., Momb, J., Thomas, P.W., Moulin, A., Petsko, G.A., Fast, W., Ringe, D.
Keywords : Zinc Bimetallohydrolase, Qourum Quenching, N-Acyl Homocysteine Thiolactone, Product Complex, AHL Lactonase, General Acid, Catalytic Mechanism, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.30 Å )
Citation :

Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures.

Liu, D.,Momb, J.,Thomas, P.W.  et al.
(2008)  Biochemistry  47 : 7706 - 7714

PubMed: 18627129
DOI: 10.1021/bi800368y

Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis: 2. Substrate Modeling and Active Site Mutations

Momb, J.,Wang, C.,Liu, D.  et al.
To be Published 

Chain : A
UniProt : Q7B8B9 (multiple entry names are found)
Reaction : -