Chlorine in PDB 5kq3: Crystal Structure of the D141A/Q233E Variant of Catalase-Peroxidase From B. Pseudomallei

All present enzymatic activity of Crystal Structure of the D141A/Q233E Variant of Catalase-Peroxidase From B. Pseudomallei:
1.11.1.21;

The structure of Crystal Structure of the D141A/Q233E Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kq3 was solved by P.C.Loewen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.73 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	101.044, 114.028, 174.505, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 19.5

The structure of Crystal Structure of the D141A/Q233E Variant of Catalase-Peroxidase From B. Pseudomallei also contains other interesting chemical elements:

Iron	(Fe)	2 atoms
Sodium	(Na)	2 atoms

The binding sites of Chlorine atom in the Crystal Structure of the D141A/Q233E Variant of Catalase-Peroxidase From B. Pseudomallei (pdb code 5kq3). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the D141A/Q233E Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kq3:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the D141A/Q233E Variant of Catalase-Peroxidase From B. Pseudomallei


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the D141A/Q233E Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl803 b:50.5 occ:1.00 O A:HOH1384 2.8 23.8 1.0 O A:HOH1415 3.2 25.2 1.0 O A:HOH1483 3.2 23.9 1.0 N A:GLY124 3.3 19.6 1.0 CB A:GLU198 3.5 45.5 1.0 CG A:GLU198 3.5 55.8 1.0 CG2 A:VAL200 3.6 30.0 1.0 CA A:GLY124 4.0 19.2 1.0 OE1 A:GLU128 4.2 33.1 1.0 CB A:ARG123 4.3 22.4 1.0 C A:ARG123 4.3 20.9 1.0 CA A:ARG123 4.3 20.6 1.0 CD A:GLU198 4.4 62.6 1.0 NA A:NA802 4.6 20.8 1.0 O A:HOH943 4.6 44.2 1.0 CG A:ARG123 4.7 22.0 1.0 O A:GLY124 4.7 19.9 1.0 C A:GLY124 4.8 19.2 1.0 CD A:GLU128 4.8 31.4 1.0 CG A:GLN130 4.9 23.3 1.0 OE2 A:GLU198 4.9 55.8 1.0 O A:HOH1245 4.9 27.7 1.0 OE2 A:GLU128 4.9 40.8 1.0 CA A:GLU198 5.0 37.2 1.0 CB A:VAL200 5.0 33.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the D141A/Q233E Variant of Catalase-Peroxidase From B. Pseudomallei


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the D141A/Q233E Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl803 b:33.9 occ:0.50 OE1 B:GLU198 0.7 30.1 0.5 CD B:GLU198 1.5 30.5 0.5 OE2 B:GLU198 2.1 31.0 0.5 CG B:GLU198 2.9 30.4 0.5 O B:HOH1290 2.9 19.6 1.0 O B:HOH1101 3.0 23.0 1.0 O B:HOH1352 3.0 27.2 1.0 N B:GLY124 3.0 20.1 1.0 CB B:GLU198 3.5 28.9 0.5 CG2 B:VAL200 3.6 26.4 1.0 CB B:GLU198 3.7 32.1 0.5 CA B:GLY124 3.7 20.0 1.0 CG B:GLU198 3.8 34.1 0.5 C B:ARG123 4.1 18.4 1.0 CB B:ARG123 4.2 18.8 1.0 CA B:ARG123 4.2 18.1 1.0 O B:HOH907 4.3 46.4 1.0 OE1 B:GLU128 4.4 34.2 1.0 C B:GLY124 4.4 19.9 1.0 NA B:NA802 4.5 21.8 1.0 O B:GLY124 4.5 21.5 1.0 CD B:GLU198 4.6 36.2 0.5 CG B:ARG123 4.8 19.7 1.0 CD B:GLU128 4.8 34.6 1.0 CG B:GLN130 4.8 22.6 1.0 O B:HOH1131 4.9 17.0 1.0 O B:HOH1259 4.9 21.3 1.0 O B:HOH1138 4.9 28.3 1.0 OE2 B:GLU128 4.9 43.8 1.0

M.Machuqueiro, B.Victor, J.Switala, J.Villanueva, C.Rovira, I.Fita, P.C.Loewen. The Catalase Activity of Catalase-Peroxidases Is Modulated By Changes in the Pka of the Distal Histidine. Biochemistry V. 56 2271 2017.
ISSN: ISSN 1520-4995
PubMed: 28409923
DOI: 10.1021/ACS.BIOCHEM.6B01276