Zinc in PDB 2oql: Structure of Phosphotriesterase Mutant H254Q/H257F

All present enzymatic activity of Structure of Phosphotriesterase Mutant H254Q/H257F:
3.1.8.1;

The structure of Structure of Phosphotriesterase Mutant H254Q/H257F, PDB code: 2oql was solved by J.Kim, 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)	50.00 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	43.528, 45.367, 79.113, 104.75, 93.13, 97.97
R / Rfree (%)	14.6 / 18.9

The binding sites of Zinc atom in the Structure of Phosphotriesterase Mutant H254Q/H257F (pdb code 2oql). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure of Phosphotriesterase Mutant H254Q/H257F, PDB code: 2oql:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Structure of Phosphotriesterase Mutant H254Q/H257F


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Phosphotriesterase Mutant H254Q/H257F within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:17.4 occ:1.00 NE2 A:HIS57 2.1 10.2 1.0 OQ1 A:KCX169 2.1 12.4 1.0 OD1 A:ASP301 2.2 10.4 1.0 NE2 A:HIS55 2.2 9.0 1.0 O A:HOH856 2.2 14.3 1.0 O1 A:GOL802 2.4 34.2 1.0 CX A:KCX169 3.0 12.2 1.0 CE1 A:HIS57 3.0 11.2 1.0 CD2 A:HIS55 3.0 9.0 1.0 CG A:ASP301 3.1 10.4 1.0 CD2 A:HIS57 3.1 10.6 1.0 C1 A:GOL802 3.2 33.6 1.0 CE1 A:HIS55 3.2 9.5 1.0 OD2 A:ASP301 3.3 12.4 1.0 OQ2 A:KCX169 3.5 12.2 1.0 ZN A:ZN402 3.8 17.5 0.8 NZ A:KCX169 4.0 10.2 1.0 CG2 A:VAL101 4.2 10.7 1.0 ND1 A:HIS57 4.2 9.9 1.0 CG A:HIS57 4.2 9.8 1.0 CG A:HIS55 4.2 8.6 1.0 O A:HOH1098 4.3 15.8 1.0 ND1 A:HIS55 4.3 8.8 1.0 CE1 A:HIS230 4.3 10.0 1.0 O A:HOH980 4.4 22.8 1.0 CB A:ASP301 4.4 10.5 1.0 NE2 A:HIS230 4.5 8.6 1.0 C2 A:GOL802 4.6 33.0 1.0 O A:HOH1104 4.6 46.4 1.0 CA A:ASP301 4.9 10.1 1.0 O2 A:GOL802 4.9 33.8 1.0

Zinc binding site 2 out of 4 in the Structure of Phosphotriesterase Mutant H254Q/H257F


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Phosphotriesterase Mutant H254Q/H257F within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:17.5 occ:0.80 OQ2 A:KCX169 2.0 12.2 1.0 NE2 A:HIS230 2.1 8.6 1.0 O A:HOH1098 2.2 15.8 1.0 O A:HOH856 2.2 14.3 1.0 ND1 A:HIS201 2.2 11.3 1.0 O A:HOH988 2.5 25.2 1.0 CX A:KCX169 3.0 12.2 1.0 CD2 A:HIS230 3.0 10.1 1.0 CE1 A:HIS201 3.1 13.5 1.0 CE1 A:HIS230 3.2 10.0 1.0 CG A:HIS201 3.3 12.3 1.0 OQ1 A:KCX169 3.4 12.4 1.0 CB A:HIS201 3.7 10.8 1.0 ZN A:ZN401 3.8 17.4 1.0 NE1 A:TRP131 4.2 14.5 1.0 NZ A:KCX169 4.2 10.2 1.0 CG A:HIS230 4.2 9.1 1.0 ND1 A:HIS230 4.2 9.4 1.0 O A:HOH1039 4.3 29.5 1.0 NE2 A:HIS201 4.3 12.8 1.0 OD2 A:ASP301 4.3 12.4 1.0 CE1 A:HIS55 4.3 9.5 1.0 NE2 A:HIS55 4.3 9.0 1.0 CD2 A:HIS201 4.4 11.6 1.0 O1 A:GOL802 4.4 34.2 1.0 O A:HOH943 4.4 20.6 1.0 O A:HOH1104 4.6 46.4 1.0 CA A:HIS201 4.6 10.4 1.0 O2 A:GOL802 4.7 33.8 1.0 C1 A:GOL802 4.7 33.6 1.0 NE2 A:GLN254 4.7 13.9 1.0 CE A:KCX169 4.7 9.0 1.0 CD1 A:TRP131 4.9 13.5 1.0

Zinc binding site 3 out of 4 in the Structure of Phosphotriesterase Mutant H254Q/H257F


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of Phosphotriesterase Mutant H254Q/H257F within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:17.1 occ:0.90 NE2 B:HIS57 2.1 8.7 1.0 O B:HOH1041 2.1 16.1 1.0 NE2 B:HIS55 2.2 9.7 1.0 OQ1 B:KCX169 2.2 13.6 1.0 OD1 B:ASP301 2.2 10.3 1.0 O3 B:GOL803 2.7 54.4 1.0 CD2 B:HIS55 3.0 11.0 1.0 CE1 B:HIS57 3.0 9.9 1.0 CD2 B:HIS57 3.1 9.6 1.0 CG B:ASP301 3.1 11.6 1.0 CX B:KCX169 3.1 13.9 1.0 CE1 B:HIS55 3.3 10.7 1.0 C3 B:GOL803 3.3 54.4 1.0 OD2 B:ASP301 3.3 11.7 1.0 OQ2 B:KCX169 3.6 11.5 1.0 ZN B:ZN402 3.8 19.6 0.8 NZ B:KCX169 4.1 13.2 1.0 ND1 B:HIS57 4.1 10.0 1.0 CG2 B:VAL101 4.2 10.9 1.0 CG B:HIS57 4.2 9.1 1.0 CG B:HIS55 4.2 10.9 1.0 O B:HOH1038 4.2 16.6 1.0 CE1 B:HIS230 4.3 10.3 1.0 ND1 B:HIS55 4.3 9.9 1.0 O1 B:GOL803 4.4 54.8 1.0 CB B:ASP301 4.4 10.7 1.0 O B:HOH941 4.5 21.7 1.0 NE2 B:HIS230 4.6 9.1 1.0 C2 B:GOL803 4.7 54.4 1.0 CA B:ASP301 4.9 10.8 1.0 C1 B:GOL803 5.0 54.6 1.0 O B:HOH1027 5.0 24.2 1.0

Zinc binding site 4 out of 4 in the Structure of Phosphotriesterase Mutant H254Q/H257F


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of Phosphotriesterase Mutant H254Q/H257F within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:19.6 occ:0.80 OQ2 B:KCX169 2.0 11.5 1.0 O B:HOH1038 2.1 16.6 1.0 NE2 B:HIS230 2.1 9.1 1.0 O B:HOH1041 2.2 16.1 1.0 O B:HOH1027 2.3 24.2 1.0 ND1 B:HIS201 2.4 14.5 1.0 CX B:KCX169 3.1 13.9 1.0 CE1 B:HIS230 3.1 10.3 1.0 CD2 B:HIS230 3.1 10.3 1.0 CE1 B:HIS201 3.2 15.2 1.0 OQ1 B:KCX169 3.3 13.6 1.0 CG B:HIS201 3.4 14.7 1.0 CB B:HIS201 3.8 13.8 1.0 ZN B:ZN401 3.8 17.1 0.9 NE1 B:TRP131 4.1 14.5 1.0 O1 B:GOL803 4.1 54.8 1.0 ND1 B:HIS230 4.2 10.1 1.0 CG B:HIS230 4.3 10.5 1.0 NE2 B:HIS55 4.3 9.7 1.0 NZ B:KCX169 4.3 13.2 1.0 OD2 B:ASP301 4.3 11.7 1.0 CE1 B:HIS55 4.3 10.7 1.0 O B:HOH1092 4.4 30.4 1.0 NE2 B:HIS201 4.4 15.0 1.0 C3 B:GOL803 4.5 54.4 1.0 CD2 B:HIS201 4.5 13.6 1.0 O B:HOH1040 4.6 26.8 1.0 CA B:HIS201 4.6 14.0 1.0 O3 B:GOL803 4.6 54.4 1.0 NE2 B:GLN254 4.7 16.5 1.0 CD1 B:TRP131 4.8 14.1 1.0 CE B:KCX169 4.8 12.0 1.0 C2 B:GOL803 5.0 54.4 1.0

J.Kim, F.M.Raushel, S.C.Almo. Crystal Structure of Pte Mutant H254Q/H257F To Be Published.