Zinc in PDB 2ob3: Structure of Phosphotriesterase Mutant H257Y/L303T

All present enzymatic activity of Structure of Phosphotriesterase Mutant H257Y/L303T:
3.1.8.1;

The structure of Structure of Phosphotriesterase Mutant H257Y/L303T, PDB code: 2ob3 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)	30.00 / 1.04
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	43.362, 45.374, 79.211, 104.86, 93.27, 97.81
R / Rfree (%)	10.5 / 12.7

The binding sites of Zinc atom in the Structure of Phosphotriesterase Mutant H257Y/L303T (pdb code 2ob3). 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 H257Y/L303T, PDB code: 2ob3:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Structure of Phosphotriesterase Mutant H257Y/L303T


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 H257Y/L303T within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn901 b:5.1 occ:1.00 O A:HOH1143 2.0 7.4 1.0 NE2 A:HIS57 2.0 4.8 1.0 NE2 A:HIS55 2.1 4.5 1.0 OQ2 A:KCX169 2.1 5.5 1.0 OD1 A:ASP301 2.2 5.1 1.0 CD2 A:HIS55 3.0 4.7 1.0 CE1 A:HIS57 3.0 4.8 1.0 CX A:KCX169 3.0 5.2 1.0 CG A:ASP301 3.1 4.9 1.0 CD2 A:HIS57 3.1 4.6 1.0 CE1 A:HIS55 3.1 5.0 1.0 OD2 A:ASP301 3.3 7.5 1.0 O A:HOH1061 3.5 18.9 1.0 OQ1 A:KCX169 3.5 7.2 1.0 ZN A:ZN902 3.8 7.3 0.9 NZ A:KCX169 4.0 5.8 1.0 CG2 A:VAL101 4.0 5.7 1.0 ND1 A:HIS57 4.1 4.9 1.0 CG A:HIS55 4.2 4.5 1.0 ND1 A:HIS55 4.2 4.8 1.0 CG A:HIS57 4.2 4.2 1.0 CE1 A:HIS230 4.2 5.9 1.0 O A:HOH973 4.3 8.6 1.0 CB A:ASP301 4.4 4.6 1.0 NE2 A:HIS230 4.4 6.1 1.0 CA A:ASP301 5.0 4.5 1.0 O A:HOH1028 5.0 14.7 1.0 O A:HOH1078 5.0 22.5 1.0

Zinc binding site 2 out of 4 in the Structure of Phosphotriesterase Mutant H257Y/L303T


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 H257Y/L303T within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn902 b:7.3 occ:0.95 NE2 A:HIS230 2.0 6.1 1.0 OQ1 A:KCX169 2.0 7.2 1.0 O A:HOH973 2.1 8.6 1.0 ND1 A:HIS201 2.1 6.5 1.0 O A:HOH1143 2.3 7.4 1.0 O A:HOH1028 2.4 14.7 1.0 CE1 A:HIS201 3.0 7.6 1.0 CE1 A:HIS230 3.0 5.9 1.0 CD2 A:HIS230 3.1 5.7 1.0 CX A:KCX169 3.1 5.2 1.0 CG A:HIS201 3.2 6.5 1.0 OQ2 A:KCX169 3.4 5.5 1.0 CB A:HIS201 3.7 6.8 1.0 ZN A:ZN901 3.8 5.1 1.0 O A:HOH1061 4.0 18.9 1.0 NE1 A:TRP131 4.1 7.9 1.0 NE2 A:HIS201 4.2 9.3 1.0 O A:HOH1127 4.2 29.1 1.0 ND1 A:HIS230 4.2 5.7 1.0 CG A:HIS230 4.2 5.5 1.0 NZ A:KCX169 4.2 5.8 1.0 OD2 A:ASP301 4.3 7.5 1.0 CD2 A:HIS201 4.3 8.6 1.0 CE1 A:HIS55 4.3 5.0 1.0 NE2 A:HIS55 4.3 4.5 1.0 CA A:HIS201 4.6 5.0 1.0 O A:HOH1219 4.6 25.0 1.0 CE A:KCX169 4.7 6.0 1.0 CD1 A:TRP131 4.8 6.6 1.0 NE2 A:HIS254 5.0 9.6 1.0

Zinc binding site 3 out of 4 in the Structure of Phosphotriesterase Mutant H257Y/L303T


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 H257Y/L303T within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn903 b:4.8 occ:1.00 O B:HOH1332 2.0 6.9 1.0 NE2 B:HIS55 2.0 4.3 1.0 NE2 B:HIS57 2.0 4.2 1.0 OQ1 B:KCX169 2.0 5.1 1.0 OD1 B:ASP301 2.2 4.6 1.0 CD2 B:HIS55 3.0 4.5 1.0 CE1 B:HIS57 3.0 4.2 1.0 CX B:KCX169 3.0 5.1 1.0 CE1 B:HIS55 3.1 4.6 1.0 CD2 B:HIS57 3.1 4.0 1.0 CG B:ASP301 3.1 4.9 1.0 OD2 B:ASP301 3.3 7.1 1.0 OQ2 B:KCX169 3.4 6.4 1.0 O B:HOH1032 3.5 17.1 1.0 O B:HOH1155 3.5 25.7 1.0 ZN B:ZN904 3.7 7.3 1.0 NZ B:KCX169 4.0 5.4 1.0 CG2 B:VAL101 4.0 5.3 1.0 ND1 B:HIS57 4.1 4.5 1.0 CG B:HIS55 4.2 4.4 1.0 ND1 B:HIS55 4.2 4.4 1.0 CE1 B:HIS230 4.2 5.5 1.0 CG B:HIS57 4.2 4.2 1.0 O B:HOH1337 4.3 9.2 1.0 NE2 B:HIS230 4.4 5.7 1.0 CB B:ASP301 4.4 4.2 1.0 O B:HOH1093 4.8 20.9 1.0 O B:HOH1333 4.9 14.2 1.0 CA B:ASP301 5.0 4.3 1.0

Zinc binding site 4 out of 4 in the Structure of Phosphotriesterase Mutant H257Y/L303T


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 H257Y/L303T within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn904 b:7.3 occ:1.00 NE2 B:HIS230 2.0 5.7 1.0 OQ2 B:KCX169 2.0 6.4 1.0 O B:HOH1337 2.1 9.2 1.0 ND1 B:HIS201 2.1 5.8 1.0 O B:HOH1332 2.3 6.9 1.0 O B:HOH1333 2.4 14.2 1.0 CE1 B:HIS230 3.0 5.5 1.0 CE1 B:HIS201 3.0 7.0 1.0 CX B:KCX169 3.1 5.1 1.0 CD2 B:HIS230 3.1 5.4 1.0 CG B:HIS201 3.2 5.9 1.0 OQ1 B:KCX169 3.4 5.1 1.0 CB B:HIS201 3.7 5.6 1.0 ZN B:ZN903 3.7 4.8 1.0 O B:HOH1032 4.0 17.1 1.0 NE1 B:TRP131 4.1 7.7 1.0 ND1 B:HIS230 4.2 5.7 1.0 CG B:HIS230 4.2 5.2 1.0 NE2 B:HIS201 4.2 7.6 1.0 OD2 B:ASP301 4.2 7.1 1.0 NZ B:KCX169 4.2 5.4 1.0 O B:HOH1040 4.2 16.8 1.0 NE2 B:HIS55 4.3 4.3 1.0 CE1 B:HIS55 4.3 4.6 1.0 CD2 B:HIS201 4.3 7.4 1.0 O B:HOH1155 4.5 25.7 1.0 CA B:HIS201 4.5 5.1 1.0 O B:HOH1107 4.6 18.9 1.0 CE B:KCX169 4.7 5.7 1.0 CD1 B:TRP131 4.8 6.3 1.0

J.Kim, U.A.Ramagopal, P.Tsai, F.M.Raushel, S.C.Almo. Structure of Phosphotriesterase Mutant H257Y/L303T To Be Published.