Chlorine in PDB 5kqi: Crystal Structure of the L326D Variant of Catalase-Peroxidase From B. Pseudomallei

All present enzymatic activity of Crystal Structure of the L326D Variant of Catalase-Peroxidase From B. Pseudomallei:
1.11.1.21;

The structure of Crystal Structure of the L326D Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kqi 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)	48.42 / 1.87
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.793, 115.227, 174.543, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 19.8

The structure of Crystal Structure of the L326D 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 L326D Variant of Catalase-Peroxidase From B. Pseudomallei (pdb code 5kqi). 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 L326D Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kqi:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the L326D 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 L326D Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl803 b:45.2 occ:1.00 O A:HOH1379 2.9 26.5 1.0 O A:HOH1430 3.0 25.0 1.0 O A:HOH1482 3.0 21.2 1.0 O A:HOH1436 3.3 44.7 1.0 N A:GLY124 3.3 19.1 1.0 CG A:GLU198 3.4 48.1 1.0 CB A:GLU198 3.5 40.5 1.0 CG2 A:VAL200 3.6 29.5 1.0 CA A:GLY124 4.0 19.1 1.0 O A:HOH1267 4.2 49.6 1.0 OE1 A:GLU128 4.2 31.9 1.0 C A:ARG123 4.4 17.7 1.0 CB A:ARG123 4.4 18.5 1.0 CD A:GLU198 4.4 53.6 1.0 CA A:ARG123 4.4 19.0 1.0 CD A:GLU128 4.6 32.8 1.0 NA A:NA802 4.6 20.9 1.0 CG A:GLN130 4.7 23.0 1.0 C A:GLY124 4.8 17.6 1.0 O A:GLY124 4.8 17.7 1.0 OE2 A:GLU198 4.8 50.1 1.0 O A:HOH1092 4.9 21.1 1.0 OE2 A:GLU128 4.9 37.3 1.0 CG A:ARG123 4.9 20.3 1.0 CA A:GLU198 5.0 33.9 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the L326D 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 L326D Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl803 b:28.1 occ:0.50 OE1 B:GLU198 0.9 33.9 0.5 CD B:GLU198 1.5 33.0 0.5 OE2 B:GLU198 1.8 31.4 0.5 CG B:GLU198 2.9 31.6 0.5 O B:HOH1217 3.0 26.1 1.0 O B:HOH1191 3.0 21.1 1.0 N B:GLY124 3.1 20.0 1.0 O B:HOH1412 3.2 25.8 1.0 CG2 B:VAL200 3.6 26.0 1.0 CB B:GLU198 3.6 29.6 0.5 CB B:GLU198 3.7 27.4 0.5 CG B:GLU198 3.8 27.7 0.5 CA B:GLY124 3.8 19.0 1.0 O B:HOH907 4.0 40.0 1.0 C B:ARG123 4.1 21.0 1.0 CB B:ARG123 4.2 21.2 1.0 CA B:ARG123 4.3 20.8 1.0 OE1 B:GLU128 4.4 37.3 1.0 OE2 B:GLU128 4.5 45.2 1.0 O B:GLY124 4.6 20.4 1.0 C B:GLY124 4.6 19.3 1.0 CD B:GLU198 4.6 27.5 0.5 NA B:NA802 4.6 20.1 1.0 CD B:GLU128 4.7 34.8 1.0 CG B:ARG123 4.8 22.1 1.0 O B:HOH1334 4.8 24.7 1.0 CG B:GLN130 4.8 22.4 1.0 O B:HOH1065 4.9 16.0 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