Arsenic in PDB 4gy1: Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate

All present enzymatic activity of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate:
3.1.8.1;

The structure of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate, PDB code: 4gy1 was solved by C.J.Jackson, N.Tokuriki, D.S.Tawfik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.60 / 1.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.223, 87.019, 88.939, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 21.5

The structure of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate also contains other interesting chemical elements:

Zinc

(Zn)

6 atoms

The binding sites of Arsenic atom in the Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate (pdb code 4gy1). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate, PDB code: 4gy1:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate within 5.0Å range: probe atom residue distance (Å) B Occ A:As404 b:33.9 occ:0.45 AS A:CAC404 0.0 33.9 0.5 O1 A:CAC404 1.7 14.6 0.5 O2 A:CAC404 1.7 14.7 0.5 C2 A:CAC404 2.0 30.0 0.5 C1 A:CAC404 2.0 16.8 0.5 ZN A:ZN402 2.8 16.1 0.4 O A:HOH643 3.1 22.4 0.8 ZN A:ZN401 3.1 16.5 0.8 OQ2 A:KCX169 3.4 11.1 0.5 OQ1 A:KCX169 3.8 15.8 0.5 ZN A:ZN403 3.8 16.3 0.2 OD2 A:ASP301 3.9 13.5 0.6 NE1 A:TRP131 4.0 12.1 0.6 OD2 A:ASP301 4.0 12.8 0.4 O A:HOH670 4.1 32.3 1.0 CX A:KCX169 4.1 15.0 0.5 OD1 A:ASP301 4.2 12.3 0.6 NE2 A:HIS57 4.3 11.5 1.0 ND1 A:HIS201 4.3 16.4 0.5 NE1 A:TRP131 4.3 18.8 0.4 OD1 A:ASP301 4.4 9.6 0.4 NE2 A:HIS230 4.4 19.4 0.8 CG A:ASP301 4.5 12.2 0.6 CE1 A:HIS201 4.6 18.9 0.5 CE1 A:HIS230 4.6 20.0 0.2 CG A:ASP301 4.6 12.1 0.4 NE2 A:HIS230 4.6 19.3 0.2 CE2 A:TRP131 4.6 11.2 0.6 CZ2 A:TRP131 4.6 13.0 0.6 CE1 A:HIS57 4.8 10.9 1.0 CE2 A:TRP131 4.8 14.8 0.4 CZ2 A:TRP131 4.8 14.3 0.4 NH1 A:ARG254 4.8 20.7 0.5 CE1 A:HIS201 5.0 19.2 0.5 CD1 A:TRP131 5.0 15.4 0.6

Arsenic binding site 2 out of 2 in the Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate within 5.0Å range: probe atom residue distance (Å) B Occ B:As404 b:59.3 occ:0.58 AS B:CAC404 0.0 59.3 0.6 O2 B:CAC404 1.7 38.5 0.6 O1 B:CAC404 1.7 23.4 0.6 C2 B:CAC404 2.0 35.3 0.6 C1 B:CAC404 2.0 32.8 0.6 ZN B:ZN402 3.2 15.4 0.4 ZN B:ZN401 3.3 17.4 0.7 OQ1 B:KCX169 3.5 17.6 0.5 ZN B:ZN403 3.5 42.7 0.4 NE1 B:TRP131 4.0 14.7 0.6 O B:HOH785 4.1 13.3 0.5 CZ2 B:TRP131 4.1 16.8 0.4 OQ2 B:KCX169 4.2 22.1 0.5 O B:HOH695 4.2 34.0 1.0 NE1 B:TRP131 4.2 19.9 0.4 NE2 B:HIS57 4.2 15.0 1.0 CX B:KCX169 4.3 18.9 0.5 CZ2 B:TRP131 4.3 11.6 0.6 OD2 B:ASP301 4.3 14.6 0.7 CE2 B:TRP131 4.4 15.0 0.4 OD2 B:ASP301 4.4 15.9 0.3 OD1 B:ASP301 4.4 17.9 0.3 CE2 B:TRP131 4.5 11.1 0.6 OD1 B:ASP301 4.6 14.9 0.7 CE1 B:HIS57 4.7 12.1 1.0 CG B:ASP301 4.9 15.6 0.3 CD2 B:LEU106 4.9 19.5 1.0 CZ B:PHE271 4.9 23.2 0.5 CG B:ASP301 4.9 13.7 0.7 CE1 B:HIS230 4.9 23.5 0.2 NE2 B:HIS230 5.0 19.8 0.8 CZ B:PHE271 5.0 18.6 0.5

N.Tokuriki, C.J.Jackson, L.Afriat-Jurnou, K.T.Wyganowski, R.Tang, D.S.Tawfik. Diminishing Returns and Tradeoffs Constrain the Laboratory Optimization of An Enzyme Nat Commun V. 3 1257 2012.
ISSN: ESSN 2041-1723
PubMed: 23212386
DOI: 10.1038/NCOMMS2246