Arsenic in PDB 2o4q: Structure of Phosphotriesterase Mutant G60A

All present enzymatic activity of Structure of Phosphotriesterase Mutant G60A:
3.1.8.1;

The structure of Structure of Phosphotriesterase Mutant G60A, PDB code: 2o4q was solved by J.Kim, U.A.Ramagopal, P.C.Tsai, F.M.Raushel, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.64 / 1.95
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	55.295, 68.299, 90.030, 90.05, 100.42, 89.96
R / Rfree (%)	16.4 / 22.6

The structure of Structure of Phosphotriesterase Mutant G60A also contains other interesting chemical elements:

Zinc

(Zn)

8 atoms

The binding sites of Arsenic atom in the Structure of Phosphotriesterase Mutant G60A (pdb code 2o4q). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 4 binding sites of Arsenic where determined in the Structure of Phosphotriesterase Mutant G60A, PDB code: 2o4q:
Jump to Arsenic binding site number: 1; 2; 3; 4;

Arsenic binding site 1 out of 4 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range: probe atom residue distance (Å) B Occ A:As1 b:22.2 occ:0.80 AS A:CAC1 0.0 22.2 0.8 O1 A:CAC1 1.7 24.3 0.8 O2 A:CAC1 1.8 16.0 0.8 C2 A:CAC1 2.0 12.0 0.8 C1 A:CAC1 2.0 20.1 0.8 OQ1 A:KCX169 3.2 12.4 1.0 ZN A:ZN2401 3.3 16.7 1.0 ZN A:ZN2402 3.3 18.6 1.0 O A:HOH2593 3.6 22.4 1.0 CX A:KCX169 4.0 16.4 1.0 OQ2 A:KCX169 4.0 17.2 1.0 NE1 A:TRP131 4.0 12.9 1.0 O A:HOH2488 4.1 17.5 1.0 NE2 A:HIS57 4.1 13.7 1.0 CZ2 A:TRP131 4.2 12.0 1.0 CE2 A:TRP131 4.3 11.4 1.0 OD2 A:ASP301 4.5 17.7 1.0 OD1 A:ASP301 4.5 16.4 1.0 CE1 A:HIS57 4.6 10.9 1.0 O A:HOH2596 4.7 31.0 1.0 CD2 A:HIS57 4.8 11.3 1.0 NE2 A:HIS230 4.9 14.3 1.0 ND1 A:HIS201 4.9 14.5 1.0 CG A:ASP301 5.0 15.6 1.0

Arsenic binding site 2 out of 4 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range: probe atom residue distance (Å) B Occ B:As2 b:21.9 occ:0.70 AS B:CAC2 0.0 21.9 0.7 O2 B:CAC2 1.7 22.6 0.7 O1 B:CAC2 1.7 13.2 0.7 C2 B:CAC2 2.0 17.7 0.7 C1 B:CAC2 2.0 13.6 0.7 OQ2 B:KCX169 3.3 15.0 1.0 ZN B:ZN2403 3.3 18.6 1.0 ZN B:ZN2404 3.3 22.6 1.0 NE1 B:TRP131 3.9 12.8 1.0 CX B:KCX169 4.0 16.6 1.0 OQ1 B:KCX169 4.0 14.9 1.0 O B:HOH2469 4.0 21.1 1.0 NE2 B:HIS57 4.1 17.2 1.0 CZ2 B:TRP131 4.2 12.8 1.0 CE2 B:TRP131 4.3 13.5 1.0 OD2 B:ASP301 4.5 17.0 1.0 CE1 B:HIS57 4.6 14.6 1.0 OD1 B:ASP301 4.6 15.7 1.0 ND1 B:HIS201 4.9 18.3 1.0 CD2 B:HIS57 4.9 19.6 1.0 CD1 B:TRP131 4.9 16.3 1.0 NE2 B:HIS230 4.9 17.8 1.0

Arsenic binding site 3 out of 4 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range: probe atom residue distance (Å) B Occ K:As3 b:22.5 occ:0.80 AS K:CAC3 0.0 22.5 0.8 O2 K:CAC3 1.7 25.6 0.8 O1 K:CAC3 1.8 12.7 0.8 C2 K:CAC3 2.0 19.6 0.8 C1 K:CAC3 2.0 12.7 0.8 OQ1 K:KCX169 3.2 13.8 1.0 ZN K:ZN2405 3.3 14.1 0.9 ZN K:ZN2406 3.3 19.0 1.0 O K:HOH2672 3.6 23.2 1.0 CX K:KCX169 3.9 13.2 1.0 NE1 K:TRP131 4.0 15.6 1.0 OQ2 K:KCX169 4.0 11.6 1.0 NE2 K:HIS57 4.1 9.1 1.0 CZ2 K:TRP131 4.1 13.9 1.0 O K:HOH2517 4.1 21.4 1.0 CE2 K:TRP131 4.3 14.2 1.0 OD1 K:ASP301 4.5 12.7 1.0 OD2 K:ASP301 4.5 15.2 1.0 CE1 K:HIS57 4.6 8.8 1.0 NE2 K:HIS230 4.8 18.6 1.0 CD2 K:HIS57 4.9 12.4 1.0 ND1 K:HIS201 4.9 17.8 1.0

Arsenic binding site 4 out of 4 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range: probe atom residue distance (Å) B Occ P:As4 b:20.9 occ:0.70 AS P:CAC4 0.0 20.9 0.7 O2 P:CAC4 1.7 19.5 0.7 O1 P:CAC4 1.7 16.3 0.7 C2 P:CAC4 2.0 21.5 0.7 C1 P:CAC4 2.0 10.9 0.7 OQ2 P:KCX169 3.2 16.0 1.0 ZN P:ZN2408 3.3 19.7 0.9 ZN P:ZN2407 3.3 14.7 0.8 O P:HOH2566 3.7 26.5 1.0 NE1 P:TRP131 3.8 13.1 1.0 CX P:KCX169 4.0 11.7 1.0 OQ1 P:KCX169 4.0 16.9 1.0 O P:HOH2516 4.1 22.4 1.0 NE2 P:HIS57 4.1 19.2 1.0 CZ2 P:TRP131 4.1 15.5 1.0 CE2 P:TRP131 4.2 16.2 1.0 OD2 P:ASP301 4.5 19.3 1.0 CE1 P:HIS57 4.6 12.4 1.0 OD1 P:ASP301 4.6 16.2 1.0 ND1 P:HIS201 4.7 17.2 1.0 CD1 P:TRP131 4.8 15.3 1.0 CD2 P:HIS57 4.8 15.3 1.0 NE2 P:HIS230 4.9 18.3 1.0

J.Kim, P.C.Tsai, S.L.Chen, F.Himo, S.C.Almo, F.M.Raushel. Structure of Diethyl Phosphate Bound to the Binuclear Metal Center of Phosphotriesterase. Biochemistry V. 47 9497 2008.
ISSN: ISSN 0006-2960
PubMed: 18702530
DOI: 10.1021/BI800971V