Zinc in PDB 2br6: Crystal Structure of Quorum-Quenching N-Acyl Homoserine Lactone Lactonase

The structure of Crystal Structure of Quorum-Quenching N-Acyl Homoserine Lactone Lactonase, PDB code: 2br6 was solved by M.H.Kim, W.C.Choi, H.O.Kang, B.S.Kang, K.J.Kim, Z.S.Derewenda, J.K.Lee, T.K.Oh, C.H.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.00 / 1.7
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.904, 55.745, 73.855, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 22

The binding sites of Zinc atom in the Crystal Structure of Quorum-Quenching N-Acyl Homoserine Lactone Lactonase (pdb code 2br6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Quorum-Quenching N-Acyl Homoserine Lactone Lactonase, PDB code: 2br6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Quorum-Quenching N-Acyl Homoserine Lactone Lactonase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Quorum-Quenching N-Acyl Homoserine Lactone Lactonase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1251 b:20.1 occ:1.00 OD2 A:ASP191 2.1 12.1 1.0 NE2 A:HIS109 2.1 10.6 1.0 NE2 A:HIS235 2.2 17.1 1.0 O A:HOH2218 2.2 19.1 1.0 OD1 A:ASP108 2.3 15.2 1.0 O A:HSL1255 2.5 41.1 1.0 CD2 A:HIS109 3.0 9.3 1.0 CG A:ASP191 3.0 13.3 1.0 C A:HSL1255 3.0 41.2 1.0 CE1 A:HIS235 3.2 17.2 1.0 CD2 A:HIS235 3.2 15.6 1.0 OD1 A:ASP191 3.2 13.4 1.0 CE1 A:HIS109 3.2 11.4 1.0 CG A:ASP108 3.2 13.2 1.0 OD A:HSL1255 3.3 40.9 1.0 ZN A:ZN1252 3.4 23.3 1.0 OD2 A:ASP108 3.5 13.6 1.0 O A:HOH2195 4.2 30.2 1.0 CG A:HIS109 4.2 10.2 1.0 CA A:HSL1255 4.2 41.3 1.0 ND1 A:HIS109 4.3 11.1 1.0 ND1 A:HIS235 4.3 14.7 1.0 NE2 A:HIS104 4.3 10.1 1.0 CG A:HIS235 4.3 16.4 1.0 CE1 A:HIS104 4.4 10.8 1.0 CB A:ASP191 4.4 11.9 1.0 CB A:ASP108 4.6 13.0 1.0 N A:HSL1255 4.7 41.5 1.0 CE1 A:TYR194 4.7 18.1 1.0 CG A:HSL1255 4.7 41.1 1.0 OH A:TYR194 4.8 20.6 1.0 O A:HOH2039 4.8 28.7 1.0 NE2 A:HIS169 4.8 13.7 1.0 CZ A:TYR194 5.0 20.6 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Quorum-Quenching N-Acyl Homoserine Lactone Lactonase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Quorum-Quenching N-Acyl Homoserine Lactone Lactonase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1252 b:23.3 occ:1.00 O A:HOH2218 2.0 19.1 1.0 NE2 A:HIS169 2.2 13.7 1.0 NE2 A:HIS104 2.3 10.1 1.0 ND1 A:HIS106 2.3 13.2 1.0 OD A:HSL1255 2.4 40.9 1.0 OD2 A:ASP191 2.6 12.1 1.0 CD2 A:HIS169 3.0 13.8 1.0 CG A:HSL1255 3.0 41.1 1.0 CD2 A:HIS104 3.1 10.9 1.0 CE1 A:HIS106 3.2 14.5 1.0 CG A:HIS106 3.3 12.1 1.0 CE1 A:HIS169 3.3 14.8 1.0 CE1 A:HIS104 3.3 10.8 1.0 ZN A:ZN1251 3.4 20.1 1.0 C A:HSL1255 3.5 41.2 1.0 CB A:HIS106 3.6 11.4 1.0 CG A:ASP191 3.6 13.3 1.0 CB A:ASP191 3.9 11.9 1.0 NE2 A:HIS109 4.1 10.6 1.0 CD2 A:HIS109 4.1 9.3 1.0 O A:HSL1255 4.2 41.1 1.0 CG A:HIS169 4.2 13.2 1.0 CA A:HSL1255 4.2 41.3 1.0 CB A:HSL1255 4.2 41.4 1.0 ND1 A:HIS169 4.3 14.0 1.0 CG A:HIS104 4.3 9.5 1.0 NE2 A:HIS106 4.4 13.9 1.0 CD2 A:HIS106 4.4 13.0 1.0 ND1 A:HIS104 4.4 8.6 1.0 OD2 A:ASP108 4.4 13.6 1.0 OH A:TYR194 4.5 20.6 1.0 OD1 A:ASP191 4.7 13.4 1.0 OD1 A:ASP108 4.9 15.2 1.0 N A:HSL1255 5.0 41.5 1.0 CE1 A:TYR194 5.0 18.1 1.0

M.H.Kim, W.C.Choi, H.O.Kang, J.S.Lee, B.S.Kang, K.J.Kim, Z.S.Derewenda, T.K.Oh, C.H.Lee, J.K.Lee. The Molecular Structure and Catalytic Mechanism of A Quorum-Quenching N-Acyl-L-Homoserine Lactone Hydrolase. Proc.Natl.Acad.Sci.Usa V. 102 17606 2005.
ISSN: ISSN 0027-8424
PubMed: 16314577
DOI: 10.1073/PNAS.0504996102