Zinc in PDB 4pcn: Phosphotriesterase Variant R22

The structure of Phosphotriesterase Variant R22, PDB code: 4pcn was solved by C.J.Jackson, E.Campbell, M.Kaltenbach, N.Tokuriki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.44 / 1.54
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	85.900, 86.266, 88.684, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 20.5

The binding sites of Zinc atom in the Phosphotriesterase Variant R22 (pdb code 4pcn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Phosphotriesterase Variant R22, PDB code: 4pcn:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Phosphotriesterase Variant R22


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Phosphotriesterase Variant R22 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:11.4 occ:1.00 O A:HOH655 2.0 17.7 1.0 NE2 A:HIS57 2.0 11.3 1.0 NE2 A:HIS55 2.1 12.8 1.0 OQ1 A:KCX169 2.1 11.9 1.0 OD1 A:ASP301 2.3 11.1 1.0 CE1 A:HIS57 3.0 10.6 1.0 CX A:KCX169 3.0 15.0 1.0 CD2 A:HIS55 3.0 12.1 1.0 CD2 A:HIS57 3.1 10.7 1.0 CE1 A:HIS55 3.1 13.7 1.0 CG A:ASP301 3.2 14.3 1.0 ZN A:ZN403 3.3 14.9 1.0 OQ2 A:KCX169 3.4 11.9 1.0 OD2 A:ASP301 3.5 14.9 1.0 O A:HOH630 3.5 7.8 1.0 CG2 A:VAL101 4.0 10.9 1.0 NZ A:KCX169 4.0 16.7 1.0 ND1 A:HIS57 4.1 10.0 1.0 CE1 A:HIS230 4.2 16.5 1.0 CG A:HIS57 4.2 9.2 1.0 CG A:HIS55 4.2 10.6 1.0 ND1 A:HIS55 4.2 12.8 1.0 NE2 A:HIS230 4.2 15.4 1.0 CB A:ASP301 4.5 10.6 1.0 O A:HOH635 4.9 32.8 1.0 CA A:ASP301 5.0 10.8 1.0

Zinc binding site 2 out of 4 in the Phosphotriesterase Variant R22


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Phosphotriesterase Variant R22 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:14.9 occ:0.98 OQ2 A:KCX169 1.9 11.9 1.0 ND1 A:HIS201 2.0 12.6 1.0 NE2 A:HIS230 2.0 15.4 1.0 O A:HOH655 2.1 17.7 1.0 CX A:KCX169 2.8 15.0 1.0 CE1 A:HIS201 2.9 16.0 1.0 CE1 A:HIS230 3.0 16.5 1.0 CG A:HIS201 3.0 14.1 1.0 CD2 A:HIS230 3.1 13.7 1.0 OQ1 A:KCX169 3.1 11.9 1.0 ZN A:ZN402 3.3 11.4 1.0 CB A:HIS201 3.5 9.9 1.0 O A:HOH630 3.5 7.8 1.0 CE1 A:HIS55 3.7 13.7 1.0 NE2 A:HIS55 3.7 12.8 1.0 NE2 A:HIS201 4.0 17.3 1.0 NZ A:KCX169 4.0 16.7 1.0 CD2 A:HIS201 4.1 15.8 1.0 ND1 A:HIS230 4.1 17.7 1.0 CG A:HIS230 4.2 13.7 1.0 OD2 A:ASP301 4.2 14.9 1.0 CA A:HIS201 4.3 12.8 1.0 NE1 A:TRP131 4.4 17.1 1.0 CE A:KCX169 4.4 20.8 1.0 OD1 A:ASP301 4.7 11.1 1.0 CG A:ASP301 4.8 14.3 1.0 CD1 A:TRP131 4.9 19.4 1.0 ND1 A:HIS55 4.9 12.8 1.0

Zinc binding site 3 out of 4 in the Phosphotriesterase Variant R22


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Phosphotriesterase Variant R22 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn405 b:13.3 occ:0.86 OQ1 B:KCX169 1.9 15.3 1.0 O B:HOH725 1.9 16.2 1.0 ND1 B:HIS201 2.0 11.9 1.0 NE2 B:HIS230 2.0 12.2 1.0 CX B:KCX169 2.9 14.4 1.0 CE1 B:HIS201 2.9 15.8 1.0 O B:HOH701 2.9 23.1 1.0 CD2 B:HIS230 2.9 16.2 1.0 CE1 B:HIS230 3.1 13.9 1.0 CG B:HIS201 3.1 15.3 1.0 OQ2 B:KCX169 3.2 15.7 1.0 ZN B:ZN406 3.2 12.8 0.9 CB B:HIS201 3.5 15.4 1.0 CE1 B:HIS55 3.6 13.9 1.0 O2 B:MPD403 3.6 23.6 1.0 NE2 B:HIS55 3.7 11.8 1.0 NE2 B:HIS201 4.0 18.6 1.0 NZ B:KCX169 4.1 22.5 1.0 OD2 B:ASP301 4.1 12.9 1.0 CG B:HIS230 4.1 12.1 1.0 ND1 B:HIS230 4.1 12.3 1.0 CD2 B:HIS201 4.1 20.2 1.0 CA B:HIS201 4.3 15.8 1.0 CE B:KCX169 4.5 25.7 1.0 OD1 B:ASP301 4.6 12.2 1.0 CG B:ASP301 4.6 12.3 1.0 NE1 B:TRP131 4.7 16.8 1.0 C2 B:MPD403 4.7 35.9 1.0 ND1 B:HIS55 4.8 13.5 1.0 CD1 B:TRP131 4.9 17.2 1.0 CD2 B:HIS55 4.9 10.5 1.0 CM B:MPD403 5.0 28.1 1.0

Zinc binding site 4 out of 4 in the Phosphotriesterase Variant R22


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Phosphotriesterase Variant R22 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn406 b:12.8 occ:0.95 O B:HOH725 2.0 16.2 1.0 NE2 B:HIS57 2.0 11.9 1.0 NE2 B:HIS55 2.1 11.8 1.0 OQ2 B:KCX169 2.2 15.7 1.0 OD1 B:ASP301 2.2 12.2 1.0 CE1 B:HIS57 2.9 10.8 1.0 CX B:KCX169 3.0 14.4 1.0 CD2 B:HIS55 3.0 10.5 1.0 CD2 B:HIS57 3.1 12.0 1.0 CG B:ASP301 3.1 12.3 1.0 CE1 B:HIS55 3.2 13.9 1.0 ZN B:ZN405 3.2 13.3 0.9 OQ1 B:KCX169 3.4 15.3 1.0 O B:HOH701 3.4 23.1 1.0 OD2 B:ASP301 3.4 12.9 1.0 CM B:MPD403 3.6 28.1 1.0 CG2 B:VAL101 4.1 13.8 1.0 O2 B:MPD403 4.1 23.6 1.0 ND1 B:HIS57 4.1 11.5 1.0 NZ B:KCX169 4.1 22.5 1.0 NE2 B:HIS230 4.1 12.2 1.0 CE1 B:HIS230 4.2 13.9 1.0 CG B:HIS57 4.2 13.2 1.0 CG B:HIS55 4.2 9.9 1.0 ND1 B:HIS55 4.3 13.5 1.0 C2 B:MPD403 4.4 35.9 1.0 CB B:ASP301 4.4 10.8 1.0 CA B:ASP301 4.9 10.1 1.0

C.J.Jackson, E.Campbell, M.Kaltenbach, N.Tokuriki. Phosphotriesterase Variant R22 To Be Published.