Zinc in PDB 6fef: Phosphotriesterase PTE_A53_2

The structure of Phosphotriesterase PTE_A53_2, PDB code: 6fef was solved by O.Dym, N.Aggarwal, S.Albeck, T.Unger, S.Hamer Rogotner, I.Silman, H.Leader, Y.Ashani, M.Goldsmith, P.Greisen, D.Tawfik, L.J.Sussman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.92 / 1.77
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	69.669, 69.669, 186.830, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 20.1

The binding sites of Zinc atom in the Phosphotriesterase PTE_A53_2 (pdb code 6fef). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Phosphotriesterase PTE_A53_2, PDB code: 6fef:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Phosphotriesterase PTE_A53_2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Phosphotriesterase PTE_A53_2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:15.0 occ:1.00 NE2 A:HIS57 2.0 10.5 1.0 O1 A:FMT401 2.1 12.1 1.0 O A:HOH501 2.1 14.6 1.0 NE2 A:HIS55 2.1 13.8 1.0 OD1 A:ASP301 2.3 14.0 1.0 CE1 A:HIS57 3.0 12.5 1.0 CD2 A:HIS55 3.0 12.7 1.0 CD2 A:HIS57 3.1 13.2 1.0 C A:FMT401 3.1 12.6 1.0 CG A:ASP301 3.1 15.7 1.0 CE1 A:HIS55 3.2 12.4 1.0 N1 A:IMD404 3.2 27.4 1.0 C2 A:IMD404 3.2 11.4 1.0 OD2 A:ASP301 3.4 15.4 1.0 O2 A:FMT401 3.6 11.5 1.0 ZN A:ZN403 3.8 14.8 1.0 O A:HOH502 4.0 17.4 1.0 CG2 A:VAL101 4.0 10.9 1.0 ND1 A:HIS57 4.1 12.7 1.0 CG A:HIS55 4.2 12.2 1.0 CE1 A:HIS230 4.2 14.8 1.0 C5 A:IMD404 4.2 14.4 1.0 CG A:HIS57 4.2 12.5 1.0 ND1 A:HIS55 4.2 10.1 1.0 NZ A:LYS169 4.2 13.9 1.0 N3 A:IMD404 4.2 24.9 1.0 NE2 A:HIS230 4.5 12.1 1.0 CB A:ASP301 4.5 10.9 1.0 C4 A:IMD404 4.7 25.5 1.0 O A:HOH691 4.9 32.8 1.0 CA A:ASP301 5.0 12.7 1.0

Zinc binding site 2 out of 2 in the Phosphotriesterase PTE_A53_2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Phosphotriesterase PTE_A53_2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:14.8 occ:1.00 O2 A:FMT401 2.0 11.5 1.0 ND1 A:HIS201 2.0 13.4 1.0 NE2 A:HIS230 2.0 12.1 1.0 O A:HOH502 2.1 17.4 1.0 O A:HOH501 2.6 14.6 1.0 CE1 A:HIS201 2.9 16.5 1.0 C A:FMT401 3.0 12.6 1.0 CD2 A:HIS230 3.0 13.7 1.0 CE1 A:HIS230 3.0 14.8 1.0 CG A:HIS201 3.1 12.1 1.0 N1 A:IMD404 3.2 27.4 1.0 O1 A:FMT401 3.3 12.1 1.0 CB A:HIS201 3.5 10.4 1.0 ZN A:ZN402 3.8 15.0 1.0 NE1 A:TRP131 3.9 19.0 1.0 C5 A:IMD404 4.0 14.4 1.0 NE2 A:HIS201 4.1 16.7 1.0 C2 A:IMD404 4.1 11.4 1.0 O A:HOH657 4.1 24.9 1.0 ND1 A:HIS230 4.1 14.4 1.0 CG A:HIS230 4.2 12.0 1.0 CD2 A:HIS201 4.2 15.9 1.0 CE1 A:HIS55 4.2 12.4 1.0 NZ A:LYS169 4.3 13.9 1.0 CA A:HIS201 4.3 10.8 1.0 NE2 A:HIS55 4.3 13.8 1.0 CD1 A:TRP131 4.5 18.3 1.0 OD2 A:ASP301 4.6 15.4 1.0 CE A:LYS169 4.7 11.1 1.0

O.Dym, N.Aggarwal, S.Albeck, T.Unger, S.Hamer Rogotner, I.Silman, H.Leader, Y.Ashani, M.Goldsmith, P.Greisen, D.Tawfik, L.J.Sussman. Crystal Structures of Bacterial Phosphotriesterase Variants with High Catalytic Activity Towards Organophosphate Nerve Agents Developed By Use of Structure-Based Design and Molecular Evolution To Be Published.