Het-PDB Navi2 (PDB: 3DHA)

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Ligands
Code	Name	Link
C6L	N-hexanoyl-L-homoserine	PoSSuM
GOL	Glycerol	PoSSuM
ZN	Zinc ion	PoSSuM

Non-standard Residues
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Glycosylation
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Download interaction data: 3DHA

Code :

3DHA PDBj RCSB PDB PDBe

Header :

HYDROLASE

Title :

An Ultral High Resolution Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homoserine Bound at An Alternative Site

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: The fusion protein, maltose binding protein, was cut off before crystallization using TEV protease resulting in 4 extra residues at the N terminus.

Authors :

Liu, D., Momb, J., Thomas, P.W., Moulin, A., Petsko, G.A., Fast, W., Ringe, D.

Keywords :

Zinc Bimetallohydrolase, Quorum Quenching, N-Acyl Homoserine lactone, Alternative Binding Site, Product Complex, AHL Lactonase, HYDROLASE

Exp. method :

X-RAY DIFFRACTION ( 0.95 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

Mechanism of the Quorum-quenching Lactonase (AiiA) from Bacillus thuringensis: 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 :	-

PDB ID: 3DHA