Arsenic in PDB 4xd5: Phosphotriesterase Variant R2

The structure of Phosphotriesterase Variant R2, PDB code: 4xd5 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)	44.19 / 1.85
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	85.704, 85.869, 88.382, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 20.4

The structure of Phosphotriesterase Variant R2 also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Arsenic atom in the Phosphotriesterase Variant R2 (pdb code 4xd5). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Phosphotriesterase Variant R2, PDB code: 4xd5:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the Phosphotriesterase Variant R2


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Phosphotriesterase Variant R2 within 5.0Å range: probe atom residue distance (Å) B Occ A:As2403 b:26.0 occ:0.68 AS A:CAC2403 0.0 26.0 0.7 O2 A:CAC2403 1.7 18.1 0.7 O1 A:CAC2403 1.8 9.9 0.7 C2 A:CAC2403 2.0 20.5 0.7 C1 A:CAC2403 2.0 26.3 0.7 ZN A:ZN2402 3.1 14.2 0.8 ZN A:ZN2401 3.3 13.8 1.0 NH2 A:ARG254 3.5 26.5 0.3 OQ2 A:KCX169 3.5 14.6 1.0 OQ1 A:KCX169 4.0 14.3 1.0 NE1 A:TRP131 4.0 21.5 1.0 OD2 A:ASP301 4.1 15.4 1.0 CX A:KCX169 4.2 17.0 1.0 O A:HOH2650 4.3 33.7 1.0 CZ2 A:TRP131 4.3 20.5 1.0 NE2 A:HIS57 4.3 12.5 1.0 OD1 A:ASP301 4.4 9.4 1.0 CE2 A:TRP131 4.4 17.3 1.0 ND1 A:HIS201 4.5 19.0 1.0 NE2 A:HIS230 4.6 12.7 1.0 CZ A:ARG254 4.7 23.5 0.3 CG A:ASP301 4.7 10.3 1.0 CE1 A:HIS57 4.8 10.7 1.0 CE1 A:HIS201 4.8 28.6 1.0

Arsenic binding site 2 out of 2 in the Phosphotriesterase Variant R2


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Phosphotriesterase Variant R2 within 5.0Å range: probe atom residue distance (Å) B Occ G:As401 b:26.3 occ:0.79 AS G:CAC401 0.0 26.3 0.8 O1 G:CAC401 1.7 17.9 0.8 O2 G:CAC401 1.7 22.3 0.8 C1 G:CAC401 2.0 26.7 0.8 C2 G:CAC401 2.0 19.7 0.8 ZN G:ZN403 3.1 18.0 0.9 ZN G:ZN402 3.3 14.9 0.9 OQ2 G:KCX169 3.5 16.1 1.0 NH2 G:ARG254 3.8 25.9 0.3 OD2 G:ASP301 4.0 23.6 1.0 OQ1 G:KCX169 4.1 17.1 1.0 CX G:KCX169 4.2 19.8 1.0 NE2 G:HIS57 4.3 12.5 1.0 NE1 G:TRP131 4.3 18.6 1.0 O G:HOH664 4.3 43.4 1.0 NE2 G:HIS230 4.4 18.7 1.0 OD1 G:ASP301 4.4 15.8 1.0 CZ2 G:TRP131 4.5 25.9 1.0 ND1 G:HIS201 4.5 15.1 1.0 CG G:ASP301 4.6 18.4 1.0 CE2 G:TRP131 4.7 21.1 1.0 CE1 G:HIS201 4.8 25.4 1.0 CZ G:ARG254 4.9 25.9 0.3 NH1 G:ARG254 4.9 29.2 0.7 CE1 G:HIS57 4.9 15.3 1.0 CE1 G:HIS230 4.9 19.8 1.0

E.Campbell, M.Kaltenbach, G.J.Correy, P.D.Carr, B.T.Porebski, E.K.Livingstone, L.Afriat-Jurnou, A.M.Buckle, M.Weik, F.Hollfelder, N.Tokuriki, C.J.Jackson. The Role of Protein Dynamics in the Evolution of New Enzyme Function. Nat.Chem.Biol. V. 12 944 2016.
ISSN: ESSN 1552-4469
PubMed: 27618189
DOI: 10.1038/NCHEMBIO.2175