Zinc in PDB 2a7m: 1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus Thuringiensis

The structure of 1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus Thuringiensis, PDB code: 2a7m was solved by D.Liu, B.W.Lepore, G.A.Petsko, P.W.Thomas, E.M.Stone, W.Fast, D.Ringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.64 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.600, 55.551, 80.094, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 21.1

The binding sites of Zinc atom in the 1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus Thuringiensis (pdb code 2a7m). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the 1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus Thuringiensis, PDB code: 2a7m:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the 1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of 1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus Thuringiensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn251 b:18.2 occ:1.00 O A:HOH253 2.0 18.1 1.0 OD2 A:ASP191 2.0 16.7 1.0 NE2 A:HIS109 2.0 14.0 1.0 NE2 A:HIS235 2.1 19.1 1.0 OD1 A:ASP108 2.2 18.7 1.0 CD2 A:HIS109 2.9 16.2 1.0 CG A:ASP191 3.0 17.3 1.0 CE1 A:HIS235 3.1 23.4 1.0 CE1 A:HIS109 3.1 17.1 1.0 CD2 A:HIS235 3.1 22.6 1.0 CG A:ASP108 3.2 20.5 1.0 OD1 A:ASP191 3.3 18.2 1.0 ZN A:ZN252 3.3 18.0 1.0 OD2 A:ASP108 3.5 17.2 1.0 O2 A:GOL805 3.8 20.4 0.4 O A:HOH318 3.9 20.4 1.0 O2 A:GOL805 4.1 50.6 0.6 CG A:HIS109 4.1 14.1 1.0 ND1 A:HIS109 4.1 14.6 1.0 NE2 A:HIS104 4.2 16.5 1.0 CE1 A:HIS104 4.2 14.2 1.0 ND1 A:HIS235 4.2 20.5 1.0 CG A:HIS235 4.3 19.0 1.0 CB A:ASP191 4.4 17.6 1.0 O A:HOH302 4.5 20.4 1.0 CB A:ASP108 4.5 18.0 1.0 CE1 A:TYR194 4.7 26.3 1.0 NE2 A:HIS169 4.7 16.1 1.0 OH A:TYR194 4.7 28.4 1.0 O1 A:GOL805 4.8 29.4 0.4 CZ A:TYR194 4.9 27.1 1.0 C1 A:GOL805 5.0 33.6 0.4

Zinc binding site 2 out of 2 in the 1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of 1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus Thuringiensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn252 b:18.0 occ:1.00 O A:HOH253 2.1 18.1 1.0 NE2 A:HIS169 2.1 16.1 1.0 NE2 A:HIS104 2.1 16.5 1.0 ND1 A:HIS106 2.1 16.4 1.0 OD2 A:ASP191 2.6 16.7 1.0 CD2 A:HIS169 3.0 20.4 1.0 CD2 A:HIS104 3.0 14.6 1.0 CE1 A:HIS106 3.0 18.7 1.0 CE1 A:HIS104 3.1 14.2 1.0 CE1 A:HIS169 3.1 19.6 1.0 CG A:HIS106 3.2 18.2 1.0 ZN A:ZN251 3.3 18.2 1.0 CB A:HIS106 3.6 16.5 1.0 CG A:ASP191 3.6 17.3 1.0 O2 A:GOL805 3.9 50.6 0.6 NE2 A:HIS109 3.9 14.0 1.0 CB A:ASP191 4.0 17.6 1.0 CD2 A:HIS109 4.0 16.2 1.0 C2 A:GOL805 4.0 50.4 0.6 CG A:HIS169 4.2 17.2 1.0 O2 A:GOL805 4.2 20.4 0.4 NE2 A:HIS106 4.2 21.3 1.0 CG A:HIS104 4.2 15.0 1.0 C1 A:GOL805 4.2 33.6 0.4 ND1 A:HIS104 4.2 15.4 1.0 ND1 A:HIS169 4.2 19.2 1.0 CD2 A:HIS106 4.3 18.6 1.0 OD2 A:ASP108 4.4 17.2 1.0 OH A:TYR194 4.4 28.4 1.0 O3 A:GOL805 4.5 45.0 0.6 C2 A:GOL805 4.7 31.1 0.4 O1 A:GOL805 4.7 29.4 0.4 O1 A:GOL805 4.8 50.1 0.6 OD1 A:ASP191 4.8 18.2 1.0 OD1 A:ASP108 4.8 18.7 1.0 CE1 A:TYR194 4.8 26.3 1.0 CE1 A:HIS109 4.9 17.1 1.0 C3 A:GOL805 4.9 50.4 0.6

D.Liu, B.W.Lepore, G.A.Petsko, P.W.Thomas, E.M.Stone, W.Fast, D.Ringe. Three-Dimensional Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase From Bacillus Thuringiensis Proc.Natl.Acad.Sci.Usa V. 102 11882 2005.
ISSN: ISSN 0027-8424
PubMed: 16087890
DOI: 10.1073/PNAS.0505255102