Zinc in PDB 7p85: Engineered Phosphotriesterase Bdpte 10-2-C3(C59V/C227V) in Complex with Ethyl-4-Methylbenzylphosphonate

All present enzymatic activity of Engineered Phosphotriesterase Bdpte 10-2-C3(C59V/C227V) in Complex with Ethyl-4-Methylbenzylphosphonate:
3.1.8.1;

The structure of Engineered Phosphotriesterase Bdpte 10-2-C3(C59V/C227V) in Complex with Ethyl-4-Methylbenzylphosphonate, PDB code: 7p85 was solved by A.Eichinger, A.Skerra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.05 / 1.47
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	69.298, 69.298, 186.926, 90, 90, 90
R / Rfree (%)	15.7 / 17.4

The binding sites of Zinc atom in the Engineered Phosphotriesterase Bdpte 10-2-C3(C59V/C227V) in Complex with Ethyl-4-Methylbenzylphosphonate (pdb code 7p85). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Engineered Phosphotriesterase Bdpte 10-2-C3(C59V/C227V) in Complex with Ethyl-4-Methylbenzylphosphonate, PDB code: 7p85:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Engineered Phosphotriesterase Bdpte 10-2-C3(C59V/C227V) in Complex with Ethyl-4-Methylbenzylphosphonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Engineered Phosphotriesterase Bdpte 10-2-C3(C59V/C227V) in Complex with Ethyl-4-Methylbenzylphosphonate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:10.9 occ:1.00 NE2 A:HIS57 2.0 9.3 1.0 O3 A:5ZG401 2.0 10.4 0.7 NE2 A:HIS55 2.0 9.1 1.0 O2 A:FMT402 2.1 9.4 1.0 OD1 A:ASP301 2.4 11.0 1.0 CE1 A:HIS57 3.0 9.1 1.0 CD2 A:HIS55 3.0 10.0 1.0 CD2 A:HIS57 3.0 9.6 1.0 CE1 A:HIS55 3.1 9.6 1.0 C A:FMT402 3.1 9.8 1.0 P A:5ZG401 3.1 11.2 0.7 CG A:ASP301 3.2 12.0 1.0 O1 A:5ZG401 3.3 15.3 0.7 OD2 A:ASP301 3.4 13.5 1.0 O1 A:FMT402 3.5 10.3 1.0 ZN A:ZN404 3.9 10.9 1.0 O2 A:5ZG401 3.9 8.6 0.7 C9 A:5ZG401 4.0 14.3 0.7 CG2 A:VAL101 4.0 9.7 1.0 ND1 A:HIS57 4.1 9.4 1.0 NZ A:LYS169 4.1 10.7 1.0 CE1 A:HIS230 4.1 11.0 1.0 CG A:HIS55 4.2 9.5 1.0 CG A:HIS57 4.2 9.4 1.0 ND1 A:HIS55 4.2 9.9 1.0 NE2 A:HIS230 4.5 10.0 1.0 CB A:ASP301 4.5 11.4 1.0 C7 A:5ZG401 4.6 11.4 0.7 C10 A:5ZG401 4.8 15.5 0.7

Zinc binding site 2 out of 2 in the Engineered Phosphotriesterase Bdpte 10-2-C3(C59V/C227V) in Complex with Ethyl-4-Methylbenzylphosphonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Engineered Phosphotriesterase Bdpte 10-2-C3(C59V/C227V) in Complex with Ethyl-4-Methylbenzylphosphonate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn404 b:10.9 occ:1.00 O1 A:FMT402 1.9 10.3 1.0 O2 A:5ZG401 2.0 8.6 0.7 NE2 A:HIS230 2.0 10.0 1.0 ND1 A:HIS201 2.0 10.7 1.0 C A:FMT402 2.9 9.8 1.0 CE1 A:HIS201 3.0 10.9 1.0 CD2 A:HIS230 3.0 10.6 1.0 P A:5ZG401 3.0 11.2 0.7 O3 A:5ZG401 3.0 10.4 0.7 CE1 A:HIS230 3.0 11.0 1.0 CG A:HIS201 3.1 9.9 1.0 O2 A:FMT402 3.4 9.4 1.0 CB A:HIS201 3.5 9.5 1.0 NE1 A:TRP131 3.8 10.3 1.0 ZN A:ZN403 3.9 10.9 1.0 CG A:HIS230 4.1 9.9 1.0 ND1 A:HIS230 4.1 11.4 1.0 NE2 A:HIS201 4.2 10.7 1.0 NZ A:LYS169 4.2 10.7 1.0 O A:HOH653 4.2 30.5 1.0 C7 A:5ZG401 4.2 11.4 0.7 CD2 A:HIS201 4.2 10.4 1.0 O1 A:5ZG401 4.2 15.3 0.7 CD1 A:TRP131 4.3 10.1 1.0 CE1 A:HIS55 4.3 9.6 1.0 CA A:HIS201 4.4 9.5 1.0 NE2 A:HIS55 4.5 9.1 1.0 CE A:LYS169 4.5 10.2 1.0 C9 A:5ZG401 4.8 14.3 0.7 C2 A:5ZG401 4.8 12.7 0.7 C1 A:5ZG401 4.8 12.3 0.7 OD2 A:ASP301 4.9 13.5 1.0 O A:HOH707 4.9 36.0 1.0 CE2 A:TRP131 4.9 10.2 1.0

L.Job, A.Koehler, A.Eichinger, M.Testanera, B.Escher, F.Worek, A.Skerra. Structure-Function Analysis of A Highly Active Engineered Phosphotriesterase For the Detoxification of Organophosphate Nerve Agents To Be Published.