Arsenic in PDB 4xd6: Phosphotriesterase Variant E2A

The structure of Phosphotriesterase Variant E2A, PDB code: 4xd6 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)	39.28 / 1.75
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	85.739, 85.759, 88.372, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 26.9

The structure of Phosphotriesterase Variant E2A also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Arsenic atom in the Phosphotriesterase Variant E2A (pdb code 4xd6). 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 E2A, PDB code: 4xd6:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the Phosphotriesterase Variant E2A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Phosphotriesterase Variant E2A within 5.0Å range: probe atom residue distance (Å) B Occ A:As403 b:79.7 occ:1.00 AS A:CAC403 0.0 79.7 1.0 O1 A:CAC403 1.7 56.4 1.0 O2 A:CAC403 1.8 15.1 1.0 C2 A:CAC403 2.0 43.6 1.0 C1 A:CAC403 2.0 33.3 1.0 O A:HOH859 3.2 22.9 1.0 ZN A:ZN402 3.2 13.0 1.0 ZN A:ZN401 3.3 8.4 1.0 O A:HOH637 3.5 37.1 1.0 OQ2 A:KCX169 3.7 9.8 1.0 OD2 A:ASP301 3.8 13.2 1.0 O A:HOH679 4.1 28.8 1.0 OD1 A:ASP301 4.1 6.1 1.0 OQ1 A:KCX169 4.2 7.8 1.0 NE1 A:TRP131 4.2 15.2 1.0 NE2 A:HIS57 4.2 8.9 1.0 CX A:KCX169 4.4 9.6 1.0 CZ2 A:TRP131 4.4 19.0 1.0 CG A:ASP301 4.4 13.2 1.0 ND1 A:HIS201 4.6 18.5 1.0 CE2 A:TRP131 4.6 15.9 1.0 O A:HOH687 4.6 50.8 1.0 NE2 A:HIS230 4.7 8.5 1.0 CE1 A:HIS201 4.7 18.3 1.0 CE1 A:HIS57 4.8 8.1 1.0

Arsenic binding site 2 out of 2 in the Phosphotriesterase Variant E2A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Phosphotriesterase Variant E2A within 5.0Å range: probe atom residue distance (Å) B Occ G:As402 b:63.6 occ:1.00 AS G:CAC402 0.0 63.6 1.0 O2 G:CAC402 1.7 72.2 1.0 O1 G:CAC402 1.8 20.0 1.0 C1 G:CAC402 2.0 56.5 1.0 C2 G:CAC402 2.0 28.4 1.0 O G:HOH815 3.1 25.4 1.0 ZN G:ZN401 3.2 22.2 1.0 ZN G:ZN403 3.3 18.6 1.0 OQ2 G:KCX169 3.6 15.1 1.0 OD2 G:ASP301 4.1 27.1 1.0 OQ1 G:KCX169 4.2 16.7 1.0 NE2 G:HIS57 4.3 15.2 1.0 CZ2 G:TRP131 4.3 27.9 1.0 NE1 G:TRP131 4.3 23.4 1.0 CX G:KCX169 4.3 17.4 1.0 OD1 G:ASP301 4.4 20.5 1.0 CE2 G:TRP131 4.5 20.4 1.0 ND1 G:HIS201 4.6 25.8 1.0 NE2 G:HIS230 4.6 24.1 1.0 CG G:ASP301 4.7 25.2 1.0 CE1 G:HIS201 4.8 23.3 1.0 O G:HOH731 4.8 36.8 1.0 CD2 G:HIS57 4.9 13.4 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