Zinc in PDB 4pcp: Crystal Structure of Phosphotriesterase Variant R0

All present enzymatic activity of Crystal Structure of Phosphotriesterase Variant R0:
3.1.8.1;

The structure of Crystal Structure of Phosphotriesterase Variant R0, PDB code: 4pcp was solved by E.Campbell, M.Kaltenbach, N.Tokuriki, C.J.Jackson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.16 / 1.63
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.141, 86.325, 88.722, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 21.9

The structure of Crystal Structure of Phosphotriesterase Variant R0 also contains other interesting chemical elements:

Arsenic

(As)

2 atoms

The binding sites of Zinc atom in the Crystal Structure of Phosphotriesterase Variant R0 (pdb code 4pcp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Phosphotriesterase Variant R0, PDB code: 4pcp:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Phosphotriesterase Variant R0


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Phosphotriesterase Variant R0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2401 b:11.4 occ:0.82 NE2 A:HIS57 2.0 12.8 1.0 O2 A:CAC2403 2.0 14.7 0.7 NE2 A:HIS55 2.1 12.3 1.0 OD1 A:ASP301 2.1 14.8 1.0 OQ2 A:KCX169 2.2 16.2 1.0 CE1 A:HIS57 3.0 12.0 1.0 CD2 A:HIS55 3.0 13.1 1.0 CG A:ASP301 3.0 14.1 1.0 CD2 A:HIS57 3.1 12.8 1.0 CE1 A:HIS55 3.1 15.2 1.0 CX A:KCX169 3.1 19.7 1.0 OD2 A:ASP301 3.3 17.9 1.0 AS A:CAC2403 3.3 30.9 0.7 OQ1 A:KCX169 3.5 15.4 1.0 C1 A:CAC2403 3.6 17.5 0.7 ZN A:ZN2402 3.7 19.2 0.8 O A:HOH2649 3.9 24.3 1.0 CG2 A:VAL101 4.1 10.6 1.0 ND1 A:HIS57 4.1 13.8 1.0 NZ A:KCX169 4.2 20.0 1.0 CG A:HIS55 4.2 13.5 1.0 CG A:HIS57 4.2 11.9 1.0 ND1 A:HIS55 4.2 14.9 1.0 CE1 A:HIS230 4.2 20.8 1.0 O1 A:CAC2403 4.4 29.1 0.7 CB A:ASP301 4.4 11.9 1.0 NE2 A:HIS230 4.5 18.0 1.0 C2 A:CAC2403 4.8 35.4 0.7 CA A:ASP301 4.9 12.9 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of Phosphotriesterase Variant R0


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Phosphotriesterase Variant R0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2402 b:19.2 occ:0.84 OQ1 A:KCX169 2.0 15.4 1.0 NE2 A:HIS230 2.1 18.0 1.0 ND1 A:HIS201 2.1 19.5 1.0 O1 A:CAC2403 2.5 29.1 0.7 O2 A:CAC2403 2.5 14.7 0.7 CE1 A:HIS201 3.0 28.4 1.0 CE1 A:HIS230 3.0 20.8 1.0 CX A:KCX169 3.0 19.7 1.0 CD2 A:HIS230 3.1 26.5 1.0 CG A:HIS201 3.1 21.2 1.0 AS A:CAC2403 3.2 30.9 0.7 OQ2 A:KCX169 3.3 16.2 1.0 CB A:HIS201 3.5 18.5 1.0 O A:HOH2649 3.6 24.3 1.0 ZN A:ZN2401 3.7 11.4 0.8 NE1 A:TRP131 4.0 21.8 1.0 CE1 A:HIS55 4.1 15.2 1.0 NE2 A:HIS201 4.1 26.8 1.0 ND1 A:HIS230 4.1 22.6 1.0 NZ A:KCX169 4.2 20.0 1.0 NE2 A:HIS55 4.2 12.3 1.0 CD2 A:HIS201 4.2 26.9 1.0 CG A:HIS230 4.2 23.9 1.0 CA A:HIS201 4.4 16.9 1.0 OD2 A:ASP301 4.5 17.9 1.0 C1 A:CAC2403 4.6 17.5 0.7 CD1 A:TRP131 4.6 20.5 1.0 CE A:KCX169 4.6 18.1 1.0 C2 A:CAC2403 4.7 35.4 0.7

Zinc binding site 3 out of 4 in the Crystal Structure of Phosphotriesterase Variant R0


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Phosphotriesterase Variant R0 within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn2401 b:16.5 occ:1.00 O2 G:CAC2403 2.1 15.5 0.7 NE2 G:HIS57 2.1 13.4 1.0 NE2 G:HIS55 2.1 16.4 1.0 OQ1 G:KCX169 2.1 20.0 1.0 OD1 G:ASP301 2.2 18.5 1.0 CE1 G:HIS57 3.0 17.9 1.0 CD2 G:HIS55 3.0 19.2 1.0 CG G:ASP301 3.1 18.8 1.0 CD2 G:HIS57 3.1 19.9 1.0 CX G:KCX169 3.1 22.2 1.0 CE1 G:HIS55 3.2 18.1 1.0 OD2 G:ASP301 3.3 20.2 1.0 AS G:CAC2403 3.3 28.3 0.7 OQ2 G:KCX169 3.6 17.7 1.0 C1 G:CAC2403 3.7 16.7 0.7 ZN G:ZN2402 3.8 19.2 0.9 O G:HOH2679 3.9 20.2 1.0 CG2 G:VAL101 4.1 14.2 1.0 CE1 G:HIS230 4.1 16.1 1.0 NZ G:KCX169 4.1 19.9 1.0 ND1 G:HIS57 4.2 15.8 1.0 CG G:HIS55 4.2 14.4 1.0 CG G:HIS57 4.2 13.6 1.0 O1 G:CAC2403 4.2 23.1 0.7 ND1 G:HIS55 4.2 14.0 1.0 NE2 G:HIS230 4.4 20.6 1.0 CB G:ASP301 4.4 11.0 1.0 C2 G:CAC2403 4.9 26.2 0.7 CA G:ASP301 4.9 13.3 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of Phosphotriesterase Variant R0


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Phosphotriesterase Variant R0 within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn2402 b:19.2 occ:0.86 OQ2 G:KCX169 1.9 17.7 1.0 NE2 G:HIS230 2.0 20.6 1.0 ND1 G:HIS201 2.0 20.9 1.0 O1 G:CAC2403 2.3 23.1 0.7 O2 G:CAC2403 2.7 15.5 0.7 CX G:KCX169 2.9 22.2 1.0 CE1 G:HIS201 2.9 22.4 1.0 CD2 G:HIS230 3.0 21.9 1.0 CE1 G:HIS230 3.0 16.1 1.0 CG G:HIS201 3.1 18.3 1.0 AS G:CAC2403 3.2 28.3 0.7 OQ1 G:KCX169 3.2 20.0 1.0 CB G:HIS201 3.5 15.1 1.0 O G:HOH2679 3.6 20.2 1.0 ZN G:ZN2401 3.8 16.5 1.0 NE1 G:TRP131 3.9 21.0 1.0 NE2 G:HIS201 4.1 23.9 1.0 NZ G:KCX169 4.1 19.9 1.0 ND1 G:HIS230 4.1 21.4 1.0 CG G:HIS230 4.2 16.8 1.0 CE1 G:HIS55 4.2 18.1 1.0 CD2 G:HIS201 4.2 24.6 1.0 NE2 G:HIS55 4.3 16.4 1.0 CA G:HIS201 4.3 14.7 1.0 CE G:KCX169 4.6 17.7 1.0 CD1 G:TRP131 4.6 14.9 1.0 C2 G:CAC2403 4.6 26.2 0.7 C1 G:CAC2403 4.7 16.7 0.7 OD2 G:ASP301 4.7 20.2 1.0

E.Campbell, M.Kaltenbach, N.Tokuriki, C.Jackson. Crystal Structure of Phosphotriesterase Variant R0 To Be Published.