Europium in PDB 8uqy: Round 18 Arylesterase Variant of Phosphotriesterase Bound to Europium(III) Measured at 9.5 Kev

The structure of Round 18 Arylesterase Variant of Phosphotriesterase Bound to Europium(III) Measured at 9.5 Kev, PDB code: 8uqy was solved by C.W.Breeze, R.L.Frkic, E.C.Campbell, C.J.Jackson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.94 / 1.78
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	85.511, 85.889, 89.338, 90, 90, 90
R / Rfree (%)	16.1 / 20.1

The structure of Round 18 Arylesterase Variant of Phosphotriesterase Bound to Europium(III) Measured at 9.5 Kev also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Europium atom in the Round 18 Arylesterase Variant of Phosphotriesterase Bound to Europium(III) Measured at 9.5 Kev (pdb code 8uqy). This binding sites where shown within 5.0 Angstroms radius around Europium atom.
In total only one binding site of Europium was determined in the Round 18 Arylesterase Variant of Phosphotriesterase Bound to Europium(III) Measured at 9.5 Kev, PDB code: 8uqy:

Europium binding site 1 out of 1 in the Round 18 Arylesterase Variant of Phosphotriesterase Bound to Europium(III) Measured at 9.5 Kev


Mono view


Stereo pair view

A full contact list of Europium with other atoms in the Eu binding site number 1 of Round 18 Arylesterase Variant of Phosphotriesterase Bound to Europium(III) Measured at 9.5 Kev within 5.0Å range: probe atom residue distance (Å) B Occ A:Eu403 b:42.4 occ:0.16 O A:HOH582 2.2 44.8 1.0 OD1 A:ASP301 2.4 40.3 1.0 NE2 A:HIS57 2.5 35.7 1.0 H52 A:MPD402 2.5 68.1 1.0 CL A:CL404 2.6 40.0 0.6 H13 A:MPD402 2.7 71.3 1.0 HE1 A:HIS57 2.9 39.4 1.0 CE1 A:HIS57 3.0 32.8 1.0 OD2 A:ASP301 3.1 45.7 1.0 CG A:ASP301 3.1 39.7 1.0 NE2 A:HIS55 3.1 36.6 1.0 H11 A:MPD402 3.3 71.3 1.0 C1 A:MPD402 3.5 59.4 1.0 HD2 A:HIS55 3.5 39.5 1.0 C5 A:MPD402 3.5 56.7 1.0 HE1 A:HIS230 3.6 63.2 1.0 CD2 A:HIS55 3.7 32.9 1.0 CD2 A:HIS57 3.7 31.5 1.0 H51 A:MPD402 3.8 68.1 1.0 H53 A:MPD402 3.8 68.1 1.0 O A:HOH566 4.0 46.5 1.0 HE2 A:HIS230 4.0 60.8 1.0 H12 A:MPD402 4.1 71.3 1.0 HD2 A:HIS57 4.1 37.9 1.0 HG21 A:VAL101 4.1 35.7 1.0 HG23 A:VAL101 4.2 35.7 1.0 HZ2 A:LYS169 4.2 46.0 0.6 ND1 A:HIS57 4.3 31.8 1.0 CE1 A:HIS55 4.3 34.2 1.0 CE1 A:HIS230 4.3 52.7 1.0 HH11 A:ARG254 4.5 66.2 1.0 NE2 A:HIS230 4.5 50.7 1.0 CG2 A:VAL101 4.5 29.7 1.0 HE1 A:HIS55 4.6 41.1 1.0 CB A:ASP301 4.6 35.1 1.0 HZ3 A:LYS169 4.6 46.0 0.6 HZ1 A:LYS169 4.6 46.0 0.6 CG A:HIS57 4.6 28.5 1.0 C2 A:MPD402 4.6 62.7 1.0 C4 A:MPD402 4.7 62.3 1.0 HE2 A:LYS169 4.7 50.7 0.5 HG22 A:VAL101 4.7 35.7 1.0 HD21 A:LEU106 4.7 46.1 1.0 NZ A:LYS169 4.7 38.3 0.6 HA A:ASP301 4.7 38.4 1.0 HE1 A:HIS201 4.8 59.3 1.0 O2 A:MPD402 4.8 54.5 1.0 HE1 A:TRP131 4.8 41.3 1.0 O4 A:MPD402 4.9 74.0 1.0 HB2 A:ASP301 4.9 42.2 1.0 HD1 A:HIS57 4.9 38.2 1.0 CG A:HIS55 5.0 29.2 1.0

C.W.Breeze, Y.Nakano, E.C.Campbell, R.L.Frkic, D.W.Lupton, C.J.Jackson. Mononuclear Binding and Catalytic Activity of Europium(III) and Gadolinium(III) at the Active Site of the Model Metalloenzyme Phosphotriesterase. Acta Crystallogr D Struct 2024BIOL.
ISSN: ISSN 2059-7983
PubMed: 38512071
DOI: 10.1107/S2059798324002316