Zinc in PDB 2btn: Crystal Structure and Catalytic Mechanism of the Quorum- Quenching N-Acyl Homoserine Lactone Hydrolase

The structure of Crystal Structure and Catalytic Mechanism of the Quorum- Quenching N-Acyl Homoserine Lactone Hydrolase, PDB code: 2btn was solved by 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, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.63 / 2.0
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.660, 55.921, 74.057, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 23.3

The binding sites of Zinc atom in the Crystal Structure and Catalytic Mechanism of the Quorum- Quenching N-Acyl Homoserine Lactone Hydrolase (pdb code 2btn). 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 and Catalytic Mechanism of the Quorum- Quenching N-Acyl Homoserine Lactone Hydrolase, PDB code: 2btn:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure and Catalytic Mechanism of the Quorum- Quenching N-Acyl Homoserine Lactone Hydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure and Catalytic Mechanism of the Quorum- Quenching N-Acyl Homoserine Lactone Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1251 b:20.9 occ:1.00 OD2 A:ASP191 2.1 11.2 1.0 NE2 A:HIS109 2.1 12.2 1.0 NE2 A:HIS235 2.2 15.4 1.0 O A:HOH2142 2.2 19.7 1.0 OD1 A:ASP108 2.3 12.2 1.0 O A:HOH2141 2.5 34.5 1.0 CG A:ASP191 3.0 12.6 1.0 CD2 A:HIS109 3.1 9.6 1.0 CE1 A:HIS235 3.1 14.1 1.0 CE1 A:HIS109 3.2 9.5 1.0 OD1 A:ASP191 3.2 11.6 1.0 CD2 A:HIS235 3.2 13.5 1.0 CG A:ASP108 3.3 13.2 1.0 ZN A:ZN1252 3.4 22.6 1.0 OD2 A:ASP108 3.5 10.9 1.0 O A:HOH2104 3.8 32.1 1.0 O A:HOH2128 4.2 21.6 1.0 CG A:HIS109 4.2 9.4 1.0 ND1 A:HIS109 4.3 10.5 1.0 ND1 A:HIS235 4.3 15.2 1.0 CG A:HIS235 4.3 16.2 1.0 NE2 A:HIS104 4.4 10.4 1.0 CB A:ASP191 4.4 11.4 1.0 CE1 A:HIS104 4.5 8.7 1.0 CB A:ASP108 4.6 12.2 1.0 O A:HOH2018 4.7 16.9 1.0 O A:HOH2037 4.7 50.9 1.0 CE1 A:TYR194 4.9 21.9 1.0 NE2 A:HIS169 4.9 15.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure and Catalytic Mechanism of the Quorum- Quenching N-Acyl Homoserine Lactone Hydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure and Catalytic Mechanism of the Quorum- Quenching N-Acyl Homoserine Lactone Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1252 b:22.6 occ:1.00 O A:HOH2142 2.1 19.7 1.0 NE2 A:HIS169 2.3 15.4 1.0 NE2 A:HIS104 2.3 10.4 1.0 ND1 A:HIS106 2.3 14.4 1.0 OD2 A:ASP191 2.6 11.2 1.0 O A:HOH2104 2.7 32.1 1.0 CD2 A:HIS169 3.0 13.6 1.0 CD2 A:HIS104 3.2 9.9 1.0 CG A:HIS106 3.2 13.1 1.0 CE1 A:HIS106 3.2 13.9 1.0 CE1 A:HIS104 3.3 8.7 1.0 CE1 A:HIS169 3.4 14.0 1.0 ZN A:ZN1251 3.4 20.9 1.0 CB A:HIS106 3.5 11.2 1.0 CG A:ASP191 3.5 12.6 1.0 O A:HOH2141 3.8 34.5 1.0 CB A:ASP191 3.9 11.4 1.0 NE2 A:HIS109 4.0 12.2 1.0 CD2 A:HIS109 4.1 9.6 1.0 CG A:HIS169 4.3 14.1 1.0 NE2 A:HIS106 4.3 14.5 1.0 CG A:HIS104 4.3 8.6 1.0 CD2 A:HIS106 4.4 14.3 1.0 ND1 A:HIS169 4.4 16.1 1.0 ND1 A:HIS104 4.4 8.2 1.0 OD2 A:ASP108 4.5 10.9 1.0 OD1 A:ASP191 4.6 11.6 1.0 O A:HOH2037 4.9 50.9 1.0 OH A:TYR194 4.9 24.9 1.0 OD1 A:ASP108 4.9 12.2 1.0 CA A:HIS106 5.0 11.4 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