Zinc in PDB 6fu6: Phosphotriesterase PTE_C23_2

All present enzymatic activity of Phosphotriesterase PTE_C23_2:
3.1.8.1;

The structure of Phosphotriesterase PTE_C23_2, PDB code: 6fu6 was solved by O.Dym, N.Aggarwal, S.Albeck, T.Unger, S.Hamer Rogotner, I.Silman, H.Leader, Y.Ashani, M.Goldsmith, P.Greisen, D.Tawfik, L.J.Sussman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.41 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	54.660, 81.160, 70.660, 90.00, 94.83, 90.00
R / Rfree (%)	15.6 / 19.9

The binding sites of Zinc atom in the Phosphotriesterase PTE_C23_2 (pdb code 6fu6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Phosphotriesterase PTE_C23_2, PDB code: 6fu6:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in the Phosphotriesterase PTE_C23_2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Phosphotriesterase PTE_C23_2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:13.9 occ:1.00 O41 A:TA8404 2.0 14.7 1.0 NE2 A:HIS55 2.0 12.4 1.0 OD1 A:ASP301 2.1 12.8 1.0 O1 A:FMT401 2.1 13.3 1.0 NE2 A:HIS57 2.1 10.3 1.0 C4 A:TA8404 2.9 19.4 1.0 CD2 A:HIS55 3.0 12.0 1.0 CG A:ASP301 3.0 13.2 1.0 C A:FMT401 3.0 14.0 1.0 CE1 A:HIS57 3.1 10.2 1.0 CD2 A:HIS57 3.1 10.4 1.0 CE1 A:HIS55 3.1 12.6 1.0 OD2 A:ASP301 3.5 15.2 1.0 O2 A:FMT401 3.5 13.8 1.0 C41 A:TA8404 3.6 23.3 1.0 C32 A:TA8404 3.8 28.6 1.0 ZN A:ZN403 3.9 14.9 1.0 O42 A:TA8404 4.0 14.9 1.0 CG2 A:VAL101 4.0 12.5 1.0 CE1 A:HIS230 4.1 12.8 1.0 C31 A:TA8404 4.1 37.0 1.0 CG A:HIS55 4.1 11.7 1.0 NZ A:LYS169 4.1 12.5 1.0 ND1 A:HIS55 4.1 12.1 1.0 ND1 A:HIS57 4.2 10.6 1.0 CG A:HIS57 4.2 10.6 1.0 CB A:ASP301 4.3 13.2 1.0 NE2 A:HIS230 4.4 13.1 1.0 O31 A:TA8404 4.6 42.2 1.0 C3 A:TA8404 4.8 44.1 1.0 CA A:ASP301 4.9 13.0 1.0

Zinc binding site 2 out of 5 in the Phosphotriesterase PTE_C23_2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Phosphotriesterase PTE_C23_2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:14.9 occ:1.00 O42 A:TA8404 2.0 14.9 1.0 O2 A:FMT401 2.0 13.8 1.0 NE2 A:HIS230 2.0 13.1 1.0 ND1 A:HIS201 2.0 12.6 1.0 C4 A:TA8404 2.5 19.4 1.0 O41 A:TA8404 2.6 14.7 1.0 CE1 A:HIS201 3.0 13.5 1.0 CD2 A:HIS230 3.0 12.0 1.0 CE1 A:HIS230 3.0 12.8 1.0 CG A:HIS201 3.1 11.6 1.0 C A:FMT401 3.1 14.0 1.0 O1 A:FMT401 3.4 13.3 1.0 CB A:HIS201 3.5 11.2 1.0 NE1 A:TRP131 3.8 14.2 1.0 ZN A:ZN402 3.9 13.9 1.0 C41 A:TA8404 4.1 23.3 1.0 NZ A:LYS169 4.1 12.5 1.0 NE2 A:HIS201 4.1 12.8 1.0 ND1 A:HIS230 4.1 11.8 1.0 CG A:HIS230 4.1 11.8 1.0 CD2 A:HIS201 4.2 11.8 1.0 CE1 A:HIS55 4.2 12.6 1.0 CA A:HIS201 4.3 11.1 1.0 CD1 A:TRP131 4.3 13.6 1.0 O31 A:TA8404 4.4 42.2 1.0 NE2 A:HIS55 4.4 12.4 1.0 CE A:LYS169 4.6 11.6 1.0 OD2 A:ASP301 4.9 15.2 1.0 C3 A:TA8404 4.9 44.1 1.0 CE2 A:TRP131 5.0 13.8 1.0

Zinc binding site 3 out of 5 in the Phosphotriesterase PTE_C23_2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Phosphotriesterase PTE_C23_2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:53.4 occ:1.00 OG1 B:THR345 3.0 18.9 1.0 N B:SER342 3.4 18.9 1.0 CB B:THR345 3.7 18.6 1.0 OG B:SER342 3.7 20.4 1.0 CA B:VAL341 3.9 20.6 1.0 CG1 B:VAL341 3.9 21.1 1.0 CG2 B:THR345 3.9 18.1 1.0 CB B:SER342 4.1 21.6 1.0 C B:VAL341 4.2 21.1 1.0 O B:GLY340 4.3 24.1 1.0 CA B:SER342 4.4 20.2 1.0 CG2 B:ILE288 4.4 18.8 1.0 CB B:VAL341 4.5 20.2 1.0 N B:VAL341 4.9 22.5 1.0 O B:HOH528 5.0 27.2 1.0

Zinc binding site 4 out of 5 in the Phosphotriesterase PTE_C23_2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Phosphotriesterase PTE_C23_2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn403 b:15.4 occ:1.00 O42 B:TA8405 2.0 16.6 1.0 NE2 B:HIS57 2.0 12.1 1.0 O1 B:FMT402 2.1 17.1 1.0 NE2 B:HIS55 2.1 14.1 1.0 OD1 B:ASP301 2.2 14.2 1.0 C4 B:TA8405 3.0 24.8 1.0 CD2 B:HIS55 3.0 15.0 1.0 CE1 B:HIS57 3.0 12.8 1.0 CD2 B:HIS57 3.0 12.5 1.0 CG B:ASP301 3.1 13.6 1.0 C B:FMT402 3.1 17.0 1.0 CE1 B:HIS55 3.1 13.2 1.0 OD2 B:ASP301 3.4 12.5 1.0 C41 B:TA8405 3.6 29.1 1.0 O2 B:FMT402 3.6 15.8 1.0 C32 B:TA8405 3.8 33.7 1.0 ZN B:ZN404 3.9 19.8 1.0 CE1 B:HIS230 4.0 18.5 1.0 O41 B:TA8405 4.0 20.9 1.0 CG2 B:VAL101 4.1 13.6 1.0 ND1 B:HIS57 4.1 14.0 1.0 C31 B:TA8405 4.1 42.3 1.0 CG B:HIS55 4.2 13.2 1.0 CG B:HIS57 4.2 12.2 1.0 NZ B:LYS169 4.2 16.2 1.0 ND1 B:HIS55 4.2 13.7 1.0 CB B:ASP301 4.4 12.5 1.0 NE2 B:HIS230 4.4 16.7 1.0 O32 B:TA8405 4.8 59.2 1.0 C3 B:TA8405 4.9 50.9 1.0 CA B:ASP301 4.9 12.9 1.0

Zinc binding site 5 out of 5 in the Phosphotriesterase PTE_C23_2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Phosphotriesterase PTE_C23_2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn404 b:19.8 occ:1.00 NE2 B:HIS230 2.0 16.7 1.0 O41 B:TA8405 2.0 20.9 1.0 O2 B:FMT402 2.0 15.8 1.0 ND1 B:HIS201 2.1 17.2 1.0 C4 B:TA8405 2.5 24.8 1.0 O42 B:TA8405 2.6 16.6 1.0 CE1 B:HIS230 3.0 18.5 1.0 CD2 B:HIS230 3.0 17.2 1.0 CE1 B:HIS201 3.0 18.7 1.0 C B:FMT402 3.1 17.0 1.0 CG B:HIS201 3.1 18.0 1.0 O1 B:FMT402 3.3 17.1 1.0 CB B:HIS201 3.5 18.2 1.0 NE1 B:TRP131 3.8 18.1 1.0 ZN B:ZN403 3.9 15.4 1.0 C41 B:TA8405 4.1 29.1 1.0 ND1 B:HIS230 4.1 18.1 1.0 CG B:HIS230 4.1 17.1 1.0 NZ B:LYS169 4.2 16.2 1.0 NE2 B:HIS201 4.2 20.5 1.0 CD2 B:HIS201 4.2 20.6 1.0 CE1 B:HIS55 4.3 13.2 1.0 CA B:HIS201 4.3 17.3 1.0 CD1 B:TRP131 4.4 18.6 1.0 NE2 B:HIS55 4.4 14.1 1.0 O32 B:TA8405 4.5 59.2 1.0 CE B:LYS169 4.6 15.0 1.0 OD2 B:ASP301 4.8 12.5 1.0 C3 B:TA8405 4.9 50.9 1.0 CE2 B:TRP131 5.0 19.7 1.0

O.Dym, N.Aggarwal, S.Albeck, T.Unger, S.Hamer Rogotner, I.Silman, H.Leader, Y.Ashani, M.Goldsmith, P.Greisen, D.Tawfik, L.J.Sussman. Phosphotriesterase PTE_A53_4 To Be Published.