Arsenic in PDB 2o4m: Structure of Phosphotriesterase Mutant I106G/F132G/H257Y

All present enzymatic activity of Structure of Phosphotriesterase Mutant I106G/F132G/H257Y:
3.1.8.1;

The structure of Structure of Phosphotriesterase Mutant I106G/F132G/H257Y, PDB code: 2o4m was solved by J.Kim, U.A.Ramagopal, P.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)	28.33 / 1.64
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	56.759, 68.906, 89.670, 90.03, 100.29, 94.12
R / Rfree (%)	18.9 / 24.4

The structure of Structure of Phosphotriesterase Mutant I106G/F132G/H257Y also contains other interesting chemical elements:

Zinc

(Zn)

23 atoms

The binding sites of Arsenic atom in the Structure of Phosphotriesterase Mutant I106G/F132G/H257Y (pdb code 2o4m). 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 I106G/F132G/H257Y, PDB code: 2o4m:
Jump to Arsenic binding site number: 1; 2; 3; 4;

Arsenic binding site 1 out of 4 in the Structure of Phosphotriesterase Mutant I106G/F132G/H257Y


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 I106G/F132G/H257Y within 5.0Å range: probe atom residue distance (Å) B Occ A:As4001 b:12.5 occ:0.80 AS A:CAC4001 0.0 12.5 0.8 O2 A:CAC4001 1.7 7.1 0.8 O1 A:CAC4001 1.8 14.0 0.8 C2 A:CAC4001 2.0 15.3 0.8 C1 A:CAC4001 2.0 10.7 0.8 ZN A:ZN3003 3.1 10.6 0.8 ZN A:ZN3001 3.2 9.8 0.8 OQ1 A:KCX169 3.5 11.7 1.0 OD2 A:ASP301 3.8 12.4 1.0 O A:HOH6413 4.1 32.2 1.0 OQ2 A:KCX169 4.1 14.0 1.0 NE2 A:HIS230 4.2 13.8 1.0 CX A:KCX169 4.3 15.7 1.0 NE1 A:TRP131 4.3 18.1 1.0 NE2 A:HIS57 4.3 11.0 1.0 OD1 A:ASP301 4.4 10.4 1.0 CG A:ASP301 4.5 13.4 1.0 CZ2 A:TRP131 4.6 18.5 1.0 CE1 A:HIS230 4.6 13.1 1.0 ND1 A:HIS201 4.6 7.3 1.0 CE2 A:TRP131 4.8 18.7 1.0 CE1 A:HIS57 4.8 11.3 1.0 NE2 A:HIS55 4.9 12.2 1.0 CE1 A:HIS201 4.9 20.0 1.0

Arsenic binding site 2 out of 4 in the Structure of Phosphotriesterase Mutant I106G/F132G/H257Y


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 I106G/F132G/H257Y within 5.0Å range: probe atom residue distance (Å) B Occ B:As4002 b:15.2 occ:0.80 AS B:CAC4002 0.0 15.2 0.8 O1 B:CAC4002 1.7 8.9 0.8 O2 B:CAC4002 1.8 16.1 0.8 C1 B:CAC4002 2.0 18.6 0.8 C2 B:CAC4002 2.0 18.1 0.8 ZN B:ZN3006 3.1 14.1 0.9 ZN B:ZN3005 3.2 12.0 0.9 OQ2 B:KCX169 3.4 12.6 1.0 OD2 B:ASP301 3.8 13.8 1.0 O B:HOH6162 4.1 22.3 1.0 OQ1 B:KCX169 4.1 15.7 1.0 NE1 B:TRP131 4.2 23.9 1.0 CX B:KCX169 4.2 14.5 1.0 NE2 B:HIS230 4.2 12.6 1.0 CH3 B:ACY6002 4.2 39.0 1.0 NE2 B:HIS57 4.3 8.5 1.0 OD1 B:ASP301 4.3 12.8 1.0 CG B:ASP301 4.5 20.1 1.0 CZ2 B:TRP131 4.6 25.6 1.0 CE1 B:HIS230 4.6 14.4 1.0 ND1 B:HIS201 4.7 16.2 1.0 CE2 B:TRP131 4.7 21.9 1.0 CE1 B:HIS57 4.8 14.1 1.0 NE2 B:HIS55 4.9 11.4 1.0 CE1 B:HIS201 4.9 19.5 1.0

Arsenic binding site 3 out of 4 in the Structure of Phosphotriesterase Mutant I106G/F132G/H257Y


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 I106G/F132G/H257Y within 5.0Å range: probe atom residue distance (Å) B Occ C:As4003 b:13.9 occ:0.75 AS C:CAC4003 0.0 13.9 0.8 O2 C:CAC4003 1.7 8.8 0.8 O1 C:CAC4003 1.7 18.2 0.8 C2 C:CAC4003 1.9 24.0 0.8 C1 C:CAC4003 1.9 14.5 0.8 ZN C:ZN3008 3.1 14.2 0.9 ZN C:ZN3007 3.3 12.1 0.9 OQ1 C:KCX169 3.6 16.3 1.0 OD2 C:ASP301 3.8 13.8 1.0 O C:HOH6288 3.8 28.4 1.0 OQ2 C:KCX169 4.1 15.7 1.0 CX C:KCX169 4.3 14.8 1.0 NE2 C:HIS230 4.3 14.7 1.0 NE1 C:TRP131 4.3 25.1 1.0 NE2 C:HIS57 4.3 9.8 1.0 OD1 C:ASP301 4.4 12.0 1.0 CG C:ASP301 4.5 16.0 1.0 ND1 C:HIS201 4.6 12.5 1.0 CZ2 C:TRP131 4.7 20.0 1.0 CE1 C:HIS230 4.7 11.8 1.0 CE2 C:TRP131 4.8 18.3 1.0 CE1 C:HIS57 4.9 12.6 1.0 NE2 C:HIS55 4.9 11.8 1.0 CE1 C:HIS201 5.0 20.4 1.0

Arsenic binding site 4 out of 4 in the Structure of Phosphotriesterase Mutant I106G/F132G/H257Y


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 I106G/F132G/H257Y within 5.0Å range: probe atom residue distance (Å) B Occ P:As4004 b:13.4 occ:0.80 AS P:CAC4004 0.0 13.4 0.8 O2 P:CAC4004 1.7 7.4 0.8 O1 P:CAC4004 1.7 14.6 0.8 C2 P:CAC4004 1.9 16.0 0.8 C1 P:CAC4004 2.0 16.2 0.8 ZN P:ZN3004 3.1 10.9 0.8 ZN P:ZN3002 3.3 8.9 0.8 OQ2 P:KCX169 3.6 16.5 1.0 OD2 P:ASP301 3.7 13.0 1.0 OQ1 P:KCX169 4.1 15.3 1.0 O P:HOH5140 4.2 27.5 1.0 CX P:KCX169 4.3 18.7 1.0 NE2 P:HIS230 4.3 13.5 1.0 OD1 P:ASP301 4.4 12.4 1.0 NE2 P:HIS57 4.4 9.7 1.0 NE1 P:TRP131 4.5 29.4 1.0 CG P:ASP301 4.5 13.4 1.0 O2 P:GOL5003 4.6 35.7 1.0 CE1 P:HIS230 4.7 11.3 1.0 ND1 P:HIS201 4.7 14.1 1.0 CZ2 P:TRP131 4.8 26.5 1.0 CE1 P:HIS57 4.9 10.7 1.0 NE2 P:HIS55 4.9 9.7 1.0 CE1 P:HIS201 4.9 21.4 1.0 CE2 P:TRP131 5.0 29.2 1.0

J.Kim, U.A.Ramagopal, P.Tsai, F.M.Raushel, S.C.Almo. Structure of Phosphotriesterase Mutant I106G/F132G/H257Y To Be Published.