Zinc in PDB 1bf6: Phosphotriesterase Homology Protein From Escherichia Coli

The structure of Phosphotriesterase Homology Protein From Escherichia Coli, PDB code: 1bf6 was solved by J.L.Buchbinder, R.C.Stephenson, T.S.Scanlan, R.J.Fletterick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.070, 80.800, 98.200, 90.00, 97.10, 90.00
R / Rfree (%)	20.4 / 24.1

The binding sites of Zinc atom in the Phosphotriesterase Homology Protein From Escherichia Coli (pdb code 1bf6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Phosphotriesterase Homology Protein From Escherichia Coli, PDB code: 1bf6:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Phosphotriesterase Homology Protein From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Phosphotriesterase Homology Protein From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:12.0 occ:1.00 NE2 A:HIS14 2.2 6.8 1.0 NE2 A:HIS12 2.3 10.8 1.0 OE2 A:GLU125 2.4 4.5 1.0 OD1 A:ASP243 2.4 2.8 1.0 CD2 A:HIS14 3.1 4.4 1.0 CD A:GLU125 3.1 6.5 1.0 CD2 A:HIS12 3.2 7.7 1.0 CE1 A:HIS14 3.2 6.8 1.0 CG A:ASP243 3.2 5.7 1.0 ZN A:ZN293 3.3 15.0 1.0 CE1 A:HIS12 3.4 10.0 1.0 OD2 A:ASP243 3.4 9.1 1.0 OE1 A:GLU125 3.8 9.1 1.0 CG A:HIS14 4.3 8.7 1.0 CB A:MET54 4.3 9.2 1.0 ND1 A:HIS14 4.3 9.3 1.0 CE1 A:HIS186 4.4 9.0 1.0 CG A:HIS12 4.4 12.6 1.0 ND1 A:HIS12 4.4 9.5 1.0 CG A:GLU125 4.5 7.7 1.0 CG2 A:THR245 4.5 7.7 1.0 NE2 A:HIS186 4.5 6.6 1.0 CB A:ASP243 4.5 5.7 1.0 CG A:MET54 4.7 10.6 1.0

Zinc binding site 2 out of 4 in the Phosphotriesterase Homology Protein From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Phosphotriesterase Homology Protein From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn293 b:15.0 occ:1.00 NE2 A:HIS186 2.2 6.6 1.0 OE1 A:GLU125 2.2 9.1 1.0 ND1 A:HIS158 2.3 12.8 1.0 CD A:GLU125 2.8 6.5 1.0 CE1 A:HIS186 3.1 9.0 1.0 CD2 A:HIS186 3.2 6.1 1.0 CG A:HIS158 3.2 10.7 1.0 CE1 A:HIS158 3.3 8.6 1.0 ZN A:ZN1 3.3 12.0 1.0 OE2 A:GLU125 3.4 4.5 1.0 CB A:HIS158 3.5 10.9 1.0 NE2 A:HIS12 3.8 10.8 1.0 CE1 A:HIS12 3.9 10.0 1.0 CG A:GLU125 4.2 7.7 1.0 OD2 A:ASP243 4.2 9.1 1.0 ND1 A:HIS186 4.2 7.2 1.0 CE1 A:TYR84 4.3 14.2 1.0 CA A:HIS158 4.3 10.7 1.0 OH A:TYR84 4.3 17.7 1.0 CG A:HIS186 4.3 8.0 1.0 CD2 A:HIS158 4.4 12.3 1.0 NE2 A:HIS158 4.4 13.4 1.0 CZ A:TYR84 4.8 14.2 1.0 CB A:GLU125 4.8 7.7 1.0 CG A:ASP243 4.9 5.7 1.0 OD1 A:ASP243 4.9 2.8 1.0

Zinc binding site 3 out of 4 in the Phosphotriesterase Homology Protein From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Phosphotriesterase Homology Protein From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn293 b:18.1 occ:1.00 NE2 B:HIS14 2.2 12.7 1.0 NE2 B:HIS12 2.3 14.7 1.0 OE2 B:GLU125 2.4 10.7 1.0 OD1 B:ASP243 2.5 7.8 1.0 CD2 B:HIS14 3.1 10.4 1.0 CD B:GLU125 3.1 10.3 1.0 CD2 B:HIS12 3.2 14.1 1.0 CE1 B:HIS14 3.2 11.3 1.0 CG B:ASP243 3.3 9.1 1.0 ZN B:ZN294 3.3 19.1 1.0 CE1 B:HIS12 3.4 11.8 1.0 OD2 B:ASP243 3.5 15.2 1.0 OE1 B:GLU125 3.7 12.9 1.0 CG B:HIS14 4.3 13.4 1.0 CB B:MET54 4.3 12.0 1.0 ND1 B:HIS14 4.3 12.8 1.0 NE2 B:HIS186 4.3 9.8 1.0 CG B:HIS12 4.4 15.4 1.0 CG2 B:THR245 4.4 14.2 1.0 CE1 B:HIS186 4.4 9.0 1.0 ND1 B:HIS12 4.5 11.3 1.0 CG B:GLU125 4.5 10.2 1.0 CB B:ASP243 4.6 10.2 1.0 CG B:MET54 4.7 13.9 1.0

Zinc binding site 4 out of 4 in the Phosphotriesterase Homology Protein From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Phosphotriesterase Homology Protein From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn294 b:19.1 occ:1.00 OE1 B:GLU125 2.2 12.9 1.0 NE2 B:HIS186 2.2 9.8 1.0 ND1 B:HIS158 2.3 15.2 1.0 CD B:GLU125 2.9 10.3 1.0 CD2 B:HIS186 3.1 4.9 1.0 CE1 B:HIS186 3.2 9.0 1.0 CG B:HIS158 3.3 15.2 1.0 CE1 B:HIS158 3.3 12.1 1.0 ZN B:ZN293 3.3 18.1 1.0 OE2 B:GLU125 3.4 10.7 1.0 CB B:HIS158 3.5 13.2 1.0 NE2 B:HIS12 3.7 14.7 1.0 CE1 B:HIS12 3.8 11.8 1.0 OH B:TYR84 4.2 22.6 1.0 OD2 B:ASP243 4.3 15.2 1.0 CG B:HIS186 4.3 7.8 1.0 CG B:GLU125 4.3 10.2 1.0 CE1 B:TYR84 4.3 19.4 1.0 ND1 B:HIS186 4.3 8.8 1.0 CA B:HIS158 4.3 12.3 1.0 NE2 B:HIS158 4.4 16.8 1.0 CD2 B:HIS158 4.4 15.1 1.0 CZ B:TYR84 4.7 20.3 1.0 CB B:GLU125 4.8 9.7 1.0 OD1 B:ASP243 4.9 7.8 1.0 CG B:ASP243 4.9 9.1 1.0 CD2 B:HIS12 5.0 14.1 1.0

J.L.Buchbinder, R.C.Stephenson, M.J.Dresser, J.W.Pitera, T.S.Scanlan, R.J.Fletterick. Biochemical Characterization and Crystallographic Structure of An Escherichia Coli Protein From the Phosphotriesterase Gene Family. Biochemistry V. 37 5096 1998.
ISSN: ISSN 0006-2960
PubMed: 9548740
DOI: 10.1021/BI971707+