Chlorine in PDB 8uqw: Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 13 Kev

The structure of Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 13 Kev, PDB code: 8uqw 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)	39.60 / 1.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	85.63, 86.215, 89.16, 90, 90, 90
R / Rfree (%)	18.4 / 20.6

The binding sites of Chlorine atom in the Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 13 Kev (pdb code 8uqw). 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 13 Kev, PDB code: 8uqw:
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 13 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 13 Kev within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:25.8 occ:0.63 HZ1 A:LYS169 2.0 30.4 0.4 HZ2 A:LYS169 2.3 30.4 0.4 NZ A:LYS169 2.4 25.3 0.4 HZ3 A:LYS169 2.4 30.4 0.4 HE1 A:HIS57 2.5 27.6 1.0 HE2 A:LYS169 2.6 24.2 0.6 HZ1 A:LYS169 3.1 23.9 0.6 HE1 A:HIS55 3.1 23.8 1.0 HD1 A:TRP131 3.2 24.2 1.0 HE1 A:HIS201 3.3 35.1 1.0 O A:HOH549 3.3 29.6 1.0 CE1 A:HIS57 3.3 22.9 1.0 HG23 A:VAL101 3.4 22.7 1.0 H13 A:MPD401 3.4 50.0 0.9 HE1 A:TRP131 3.4 26.4 1.0 O A:HOH563 3.5 27.6 1.0 CE A:LYS169 3.5 20.1 0.6 HD22 A:LEU106 3.6 25.0 1.0 CD1 A:TRP131 3.6 20.1 1.0 NZ A:LYS169 3.7 19.9 0.6 HG21 A:VAL101 3.7 22.7 1.0 NE1 A:TRP131 3.7 22.0 1.0 CE1 A:HIS55 3.7 19.8 1.0 HE2 A:HIS57 3.8 29.8 1.0 CE A:LYS169 3.9 22.0 0.4 HG2 A:LYS169 3.9 21.5 0.4 NE2 A:HIS57 3.9 24.8 1.0 HD23 A:LEU106 4.0 25.0 1.0 HD3 A:LYS169 4.0 22.9 0.6 H11 A:MPD401 4.0 50.0 0.9 HD21 A:LEU106 4.0 25.0 1.0 C1 A:MPD401 4.0 41.6 0.9 CG2 A:VAL101 4.0 18.9 1.0 CE1 A:HIS201 4.0 29.2 1.0 H12 A:MPD401 4.0 50.0 0.9 HZ2 A:LYS169 4.0 23.9 0.6 CD2 A:LEU106 4.0 20.8 1.0 HG2 A:LYS169 4.1 22.4 0.6 O A:HOH631 4.1 31.0 1.0 NE2 A:HIS55 4.1 22.3 1.0 HE3 A:LYS169 4.2 24.2 0.6 HE2 A:LYS169 4.2 26.5 0.4 CD A:LYS169 4.2 19.1 0.6 HZ3 A:LYS169 4.4 23.9 0.6 HE3 A:LYS169 4.4 26.5 0.4 ND1 A:HIS201 4.4 27.3 1.0 ND1 A:HIS57 4.5 19.8 1.0 CG A:LYS169 4.5 17.9 0.4 HG3 A:LYS169 4.5 21.5 0.4 HG22 A:VAL101 4.6 22.7 1.0 CG A:LYS169 4.6 18.6 0.6 CD A:LYS169 4.7 19.3 0.4 CG A:TRP131 4.7 20.4 1.0 HD3 A:LYS169 4.7 23.2 0.4 HB A:VAL101 4.8 22.4 1.0 O A:VAL101 4.8 20.7 1.0 OD1 A:ASP301 4.8 26.1 1.0 CE2 A:TRP131 4.9 23.5 1.0 ND1 A:HIS55 4.9 20.3 1.0 HB2 A:ALA171 4.9 31.9 1.0 HG3 A:LYS169 5.0 22.4 0.6

Chlorine binding site 2 out of 2 in the Round 18 Arylesterase Variant of Apo-Phosphotriesterase Measured at 13 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 13 Kev within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl402 b:38.6 occ:0.72 HE2 B:HIS57 2.2 40.8 1.0 HZ3 B:LYS169 2.6 41.4 0.4 H13 B:MPD401 2.7 56.4 0.8 HZ1 B:LYS169 2.8 41.4 0.4 HZ2 B:LYS169 2.9 41.4 0.4 NZ B:LYS169 3.0 34.5 0.4 NE2 B:HIS57 3.1 33.9 1.0 O B:HOH503 3.1 39.4 1.0 HE1 B:HIS55 3.2 44.2 1.0 HE1 B:HIS201 3.2 49.4 1.0 HE2 B:LYS169 3.2 40.6 0.6 H11 B:MPD401 3.3 56.4 0.8 HD22 B:LEU106 3.3 41.0 1.0 HE1 B:TRP131 3.4 40.1 1.0 C1 B:MPD401 3.4 47.0 0.8 HD1 B:TRP131 3.4 42.7 1.0 HG23 B:VAL101 3.5 41.0 1.0 HZ3 B:LYS169 3.5 40.0 0.6 H12 B:MPD401 3.5 56.4 0.8 HD21 B:LEU106 3.6 41.0 1.0 NE1 B:TRP131 3.6 33.3 1.0 CD1 B:TRP131 3.6 35.5 1.0 CD2 B:LEU106 3.8 34.1 1.0 HE1 B:HIS57 3.8 41.9 1.0 HG21 B:VAL101 3.8 41.0 1.0 CE1 B:HIS57 3.8 34.9 1.0 HD23 B:LEU106 3.8 41.0 1.0 CE1 B:HIS201 3.9 41.1 1.0 O B:HOH530 3.9 40.0 1.0 CE1 B:HIS55 4.0 36.8 1.0 CE B:LYS169 4.1 33.8 0.6 CG2 B:VAL101 4.1 34.1 1.0 O B:HOH513 4.1 38.3 1.0 CD2 B:HIS57 4.1 31.0 1.0 NZ B:LYS169 4.2 33.3 0.6 ND1 B:HIS201 4.2 35.8 1.0 O4 B:MPD401 4.3 55.0 0.8 HG2 B:LYS169 4.3 36.2 0.4 HD2 B:HIS57 4.3 37.3 1.0 CE B:LYS169 4.4 34.5 0.4 HG2 B:LYS169 4.5 38.1 0.6 HD3 B:LYS169 4.5 36.9 0.6 HO4 B:MPD401 4.5 66.1 0.8 NE2 B:HIS55 4.6 39.2 1.0 HG22 B:VAL101 4.6 41.0 1.0 CE2 B:TRP131 4.7 34.2 1.0 CG B:TRP131 4.7 28.5 1.0 HZ2 B:LYS169 4.7 40.0 0.6 HE3 B:LYS169 4.7 40.6 0.6 HE2 B:LYS169 4.8 41.5 0.4 C2 B:MPD401 4.8 44.5 0.8 HZ1 B:LYS169 4.8 40.0 0.6 CD B:LYS169 4.8 30.7 0.6 HE3 B:LYS169 4.9 41.5 0.4 OD1 B:ASP301 5.0 35.7 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