Arsenic in PDB 4xd4: Phosphotriesterase Variant E2B

The structure of Phosphotriesterase Variant E2B, PDB code: 4xd4 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)	39.31 / 1.90
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	85.560, 85.782, 88.443, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 24.3

The structure of Phosphotriesterase Variant E2B also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Arsenic atom in the Phosphotriesterase Variant E2B (pdb code 4xd4). 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 E2B, PDB code: 4xd4:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the Phosphotriesterase Variant E2B


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Phosphotriesterase Variant E2B within 5.0Å range: probe atom residue distance (Å) B Occ A:As2403 b:85.0 occ:1.00 AS A:CAC2403 0.0 85.0 1.0 O2 A:CAC2403 1.7 43.8 1.0 O1 A:CAC2403 1.7 28.2 1.0 C1 A:CAC2403 2.0 58.8 1.0 C2 A:CAC2403 2.0 42.3 1.0 ZN A:ZN2402 3.3 31.3 1.0 ZN A:ZN2401 3.4 18.9 1.0 OQ2 A:KCX169 3.7 18.4 1.0 NH2 A:ARG254 3.9 31.5 0.5 OD2 A:ASP301 3.9 24.6 1.0 O A:HOH2622 4.3 28.8 1.0 CZ2 A:TRP131 4.3 35.2 1.0 OD1 A:ASP301 4.4 17.9 1.0 NE1 A:TRP131 4.4 20.6 1.0 OQ1 A:KCX169 4.4 20.7 1.0 NE2 A:HIS57 4.4 13.4 1.0 CX A:KCX169 4.5 24.1 1.0 CG A:ASP301 4.6 16.9 1.0 CE2 A:TRP131 4.6 24.3 1.0 NE2 A:HIS230 4.6 20.4 1.0 ND1 A:HIS201 4.8 21.9 1.0 NH1 A:ARG254 4.9 37.1 0.6 CE1 A:HIS57 5.0 17.7 1.0

Arsenic binding site 2 out of 2 in the Phosphotriesterase Variant E2B


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Phosphotriesterase Variant E2B within 5.0Å range: probe atom residue distance (Å) B Occ G:As401 b:50.3 occ:1.00 AS G:CAC401 0.0 50.3 1.0 O1 G:CAC401 1.7 28.5 1.0 O2 G:CAC401 1.7 39.2 1.0 C1 G:CAC401 2.0 37.5 1.0 C2 G:CAC401 2.0 25.9 1.0 ZN G:ZN403 3.0 32.7 1.0 ZN G:ZN402 3.3 22.8 1.0 OQ2 G:KCX169 3.5 26.0 1.0 OD2 G:ASP301 4.0 23.5 1.0 OQ1 G:KCX169 4.1 23.4 1.0 CX G:KCX169 4.2 25.8 1.0 NE2 G:HIS57 4.3 15.3 1.0 NE2 G:HIS230 4.3 19.9 1.0 OD1 G:ASP301 4.3 19.6 1.0 NE1 G:TRP131 4.3 20.9 1.0 O G:HOH683 4.4 29.5 1.0 CG G:ASP301 4.6 24.4 1.0 CZ2 G:TRP131 4.6 24.0 1.0 ND1 G:HIS201 4.7 24.5 1.0 O G:HOH706 4.7 29.9 1.0 CE2 G:TRP131 4.7 24.1 1.0 CE1 G:HIS230 4.8 24.9 1.0 CE1 G:HIS57 4.9 16.2 1.0 NE2 G:HIS55 5.0 19.9 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