Chlorine in PDB 8uqx: Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 9.5 Kev

The structure of Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 9.5 Kev, PDB code: 8uqx 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)	42.93 / 1.52
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	85.868, 86.498, 89.303, 90, 90, 90
R / Rfree (%)	19.3 / 21.5

The binding sites of Chlorine atom in the Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 9.5 Kev (pdb code 8uqx). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 9.5 Kev, PDB code: 8uqx:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 9.5 Kev


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 9.5 Kev within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:27.4 occ:0.59 HZ3 A:LYS169 2.1 38.3 0.5 HZ2 A:LYS169 2.5 38.3 0.5 HE1 A:HIS57 2.5 29.7 1.0 NZ A:LYS169 2.5 31.9 0.5 HZ1 A:LYS169 2.6 38.3 0.5 HE2 A:LYS169 2.6 29.5 0.5 HE1 A:HIS55 3.1 28.3 1.0 H11 A:MPD401 3.1 51.0 1.0 HD1 A:TRP131 3.2 29.9 1.0 O A:HOH607 3.3 32.8 1.0 HE1 A:HIS201 3.3 36.9 1.0 CE1 A:HIS57 3.3 24.8 1.0 HZ1 A:LYS169 3.4 30.9 0.5 HG23 A:VAL101 3.4 26.2 1.0 HE1 A:TRP131 3.4 29.5 1.0 O A:HOH520 3.5 28.6 1.0 CE A:LYS169 3.6 24.5 0.5 HE2 A:HIS57 3.6 31.6 1.0 CD1 A:TRP131 3.6 24.9 1.0 HD22 A:LEU106 3.6 27.2 1.0 HG21 A:VAL101 3.7 26.2 1.0 NE1 A:TRP131 3.7 24.6 1.0 H12 A:MPD401 3.8 51.0 1.0 CE1 A:HIS55 3.8 23.6 1.0 NE2 A:HIS57 3.8 26.3 1.0 C1 A:MPD401 3.9 42.5 1.0 HG2 A:LYS169 3.9 26.1 0.5 NZ A:LYS169 4.0 25.8 0.5 HD23 A:LEU106 4.0 27.2 1.0 CE A:LYS169 4.0 25.2 0.5 O A:HOH624 4.0 35.7 1.0 CE1 A:HIS201 4.0 30.7 1.0 HD21 A:LEU106 4.0 27.2 1.0 CG2 A:VAL101 4.0 21.8 1.0 CD2 A:LEU106 4.1 22.6 1.0 HE3 A:LYS169 4.1 29.5 0.5 HG2 A:LYS169 4.1 25.3 0.5 NE2 A:HIS55 4.2 24.9 1.0 HE2 A:LYS169 4.3 30.2 0.5 H13 A:MPD401 4.4 51.0 1.0 HD3 A:LYS169 4.4 26.6 0.5 ND1 A:HIS201 4.4 29.6 1.0 CD A:LYS169 4.4 22.1 0.5 HZ2 A:LYS169 4.5 30.9 0.5 ND1 A:HIS57 4.5 23.0 1.0 H31 A:MPD401 4.5 60.4 1.0 HE3 A:LYS169 4.5 30.2 0.5 HZ3 A:LYS169 4.6 30.9 0.5 HD3 A:LYS169 4.6 26.8 0.5 CG A:LYS169 4.6 21.7 0.5 HG22 A:VAL101 4.7 26.2 1.0 CG A:TRP131 4.7 21.5 1.0 CD A:LYS169 4.7 22.3 0.5 CG A:LYS169 4.7 21.1 0.5 HE1 A:HIS230 4.7 39.0 1.0 HG3 A:LYS169 4.8 26.1 0.5 HB A:VAL101 4.8 24.7 1.0 CE2 A:TRP131 4.8 24.2 1.0 OD1 A:ASP301 4.8 27.3 1.0 O A:VAL101 4.9 22.9 1.0 ND1 A:HIS55 4.9 24.0 1.0 HG3 A:LYS169 4.9 25.3 0.5 HB2 A:ALA171 4.9 33.2 1.0

Chlorine binding site 2 out of 2 in the Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 9.5 Kev


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 9.5 Kev within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl402 b:44.8 occ:0.77 HE2 B:HIS57 2.3 46.9 1.0 HZ1 B:LYS169 2.5 49.9 0.5 HM1 B:MPD401 2.8 69.5 1.0 HE2 B:LYS169 2.8 46.9 0.5 HZ3 B:LYS169 2.9 49.9 0.5 O B:HOH508 3.0 45.9 1.0 NZ B:LYS169 3.0 41.6 0.5 NE2 B:HIS57 3.1 39.0 1.0 HM3 B:MPD401 3.1 69.5 1.0 HE1 B:HIS55 3.2 49.5 1.0 HZ2 B:LYS169 3.2 49.9 0.5 HE1 B:HIS201 3.2 53.9 1.0 HD22 B:LEU106 3.3 43.5 1.0 HE1 B:TRP131 3.3 45.2 1.0 CM B:MPD401 3.3 57.9 1.0 HD1 B:TRP131 3.3 46.4 1.0 HM2 B:MPD401 3.5 69.5 1.0 HG23 B:VAL101 3.5 42.6 1.0 NE1 B:TRP131 3.6 37.6 1.0 CD1 B:TRP131 3.6 38.6 1.0 CE B:LYS169 3.7 39.0 0.5 HD21 B:LEU106 3.7 43.5 1.0 HZ2 B:LYS169 3.7 46.8 0.5 HE3 B:LYS169 3.7 46.9 0.5 HG21 B:VAL101 3.7 42.6 1.0 CD2 B:LEU106 3.8 36.2 1.0 HD23 B:LEU106 3.8 43.5 1.0 CE1 B:HIS201 3.9 44.9 1.0 CE1 B:HIS57 4.0 41.2 1.0 HE1 B:HIS57 4.0 49.4 1.0 O B:HOH512 4.0 39.2 1.0 CE1 B:HIS55 4.0 41.2 1.0 CG2 B:VAL101 4.1 35.5 1.0 CD2 B:HIS57 4.1 37.2 1.0 ND1 B:HIS201 4.2 40.3 1.0 NZ B:LYS169 4.2 39.0 0.5 HG2 B:LYS169 4.3 42.0 0.5 HD2 B:HIS57 4.3 44.7 1.0 HG2 B:LYS169 4.4 40.7 0.5 O4 B:MPD401 4.4 68.7 1.0 CE B:LYS169 4.4 37.9 0.5 HG22 B:VAL101 4.5 42.6 1.0 NE2 B:HIS55 4.6 43.1 1.0 CE2 B:TRP131 4.6 39.0 1.0 HE2 B:LYS169 4.6 45.5 0.5 CG B:TRP131 4.7 32.4 1.0 HZ3 B:LYS169 4.7 46.8 0.5 C2 B:MPD401 4.8 54.3 1.0 HZ1 B:LYS169 4.8 46.8 0.5 H32 B:MPD401 4.8 74.8 1.0 HO4 B:MPD401 4.8 82.5 1.0 CD B:LYS169 4.9 35.7 0.5 HD3 B:LYS169 4.9 43.0 0.5 CG B:LYS169 5.0 35.0 0.5

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