Chlorine in PDB 5kq2: Crystal Structure of the A357D Variant of Catalase-Peroxidase From B. Pseudomallei

All present enzymatic activity of Crystal Structure of the A357D Variant of Catalase-Peroxidase From B. Pseudomallei:
1.11.1.21;

The structure of Crystal Structure of the A357D Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kq2 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)	47.78 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.827, 114.130, 174.989, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 19.1

The structure of Crystal Structure of the A357D 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 A357D Variant of Catalase-Peroxidase From B. Pseudomallei (pdb code 5kq2). 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 A357D Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kq2:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the A357D 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 A357D Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl803 b:44.1 occ:1.00 O A:HOH1432 3.0 23.0 1.0 O A:HOH1566 3.1 21.3 1.0 O A:HOH1494 3.1 23.6 1.0 N A:GLY124 3.4 18.3 1.0 CB A:GLU198 3.5 44.2 1.0 CG A:GLU198 3.6 51.9 1.0 CG2 A:VAL200 3.6 30.2 1.0 CA A:GLY124 4.1 18.7 1.0 OE1 A:GLU128 4.3 33.7 1.0 CB A:ARG123 4.3 19.3 1.0 O A:HOH1210 4.4 39.0 1.0 C A:ARG123 4.4 19.8 1.0 CD A:GLU198 4.5 54.9 1.0 CA A:ARG123 4.5 18.3 1.0 NA A:NA802 4.7 20.5 1.0 OE2 A:GLU128 4.7 38.8 1.0 OE2 A:GLU198 4.7 51.1 1.0 CG A:GLN130 4.7 23.8 1.0 CD A:GLU128 4.8 33.1 1.0 C A:GLY124 4.8 18.0 1.0 O A:GLY124 4.8 17.9 1.0 CG A:ARG123 4.8 18.5 1.0 O A:HOH1266 4.8 25.0 1.0 CA A:GLU198 5.0 36.9 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the A357D 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 A357D Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl803 b:39.9 occ:1.00 CG B:GLU198 2.9 44.9 1.0 O B:HOH1442 3.1 22.4 1.0 O B:HOH1564 3.1 19.3 1.0 O B:HOH1478 3.2 25.1 1.0 CB B:GLU198 3.4 36.8 1.0 N B:GLY124 3.4 18.9 1.0 CG2 B:VAL200 3.5 26.6 1.0 CA B:GLY124 4.0 19.8 1.0 O B:HOH1435 4.1 36.4 1.0 OE1 B:GLU128 4.2 33.6 1.0 O B:HOH1385 4.3 44.0 1.0 CB B:ARG123 4.3 20.5 1.0 CD B:GLU198 4.3 52.2 1.0 C B:ARG123 4.4 19.8 1.0 CA B:ARG123 4.5 18.4 1.0 CD B:GLU128 4.7 29.6 1.0 CG B:GLN130 4.7 22.1 1.0 OE2 B:GLU128 4.7 39.8 1.0 O B:HOH1344 4.7 22.9 1.0 C B:GLY124 4.8 18.9 1.0 NA B:NA802 4.8 22.1 1.0 O B:GLY124 4.8 21.8 1.0 CG B:ARG123 4.8 21.2 1.0 OE2 B:GLU198 4.8 49.5 1.0 CA B:GLU198 4.9 30.3 1.0 CB B:VAL200 5.0 25.2 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