Chlorine in PDB 5sx3: Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5

All present enzymatic activity of Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5:
1.11.1.21;

The structure of Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5, PDB code: 5sx3 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)	20.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	101.049, 114.847, 174.704, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 19.6

The structure of Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5 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 Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5 (pdb code 5sx3). 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 Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5, PDB code: 5sx3:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5


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 Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl803 b:46.1 occ:1.00 O A:HOH1397 2.8 33.5 1.0 O A:HOH1447 3.1 29.1 1.0 O A:HOH1512 3.1 31.0 1.0 N A:GLY124 3.2 23.6 1.0 O A:HOH1430 3.3 43.8 1.0 CG2 A:VAL200 3.5 40.3 1.0 CG A:GLU198 3.5 59.2 1.0 CB A:GLU198 3.8 48.3 1.0 CA A:GLY124 3.9 24.1 1.0 O A:HOH1370 4.1 54.8 1.0 CB A:ARG123 4.2 25.4 1.0 C A:ARG123 4.2 23.8 1.0 CA A:ARG123 4.2 24.8 1.0 O A:GLY124 4.5 24.1 1.0 NA A:NA802 4.5 28.8 1.0 C A:GLY124 4.6 24.5 1.0 CG A:ARG123 4.7 25.6 1.0 OE1 A:GLU128 4.7 40.6 1.0 CD A:GLU198 4.8 61.4 1.0 OE2 A:GLU198 4.9 59.6 1.0 CB A:VAL200 4.9 39.2 1.0 O A:HOH1188 4.9 30.8 1.0 CG A:GLN130 5.0 29.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5


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 Catalase-Peroxidase Katg of B. Pseudomaallei at pH 4.5 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl803 b:42.8 occ:1.00 O B:HOH1446 2.9 28.4 1.0 O B:HOH1547 3.1 19.4 1.0 O B:HOH1470 3.2 28.1 1.0 O B:HOH1492 3.3 38.0 1.0 N B:GLY124 3.4 23.9 1.0 CG2 B:VAL200 3.6 33.5 1.0 CB B:GLU198 3.7 40.7 1.0 CG B:GLU198 3.8 48.7 1.0 CA B:GLY124 4.0 23.7 1.0 CB B:ARG123 4.2 22.4 1.0 O B:HOH1367 4.2 53.1 1.0 C B:ARG123 4.3 24.3 1.0 CA B:ARG123 4.3 22.2 1.0 OE1 B:GLU128 4.6 37.0 1.0 CD B:GLU198 4.6 57.2 1.0 O B:GLY124 4.6 24.5 1.0 OE2 B:GLU198 4.6 54.3 1.0 NA B:NA802 4.7 26.1 1.0 C B:GLY124 4.7 23.8 1.0 CG B:ARG123 4.7 23.2 1.0 O B:HOH1269 4.8 25.7 1.0 CG B:GLN130 4.9 22.9 1.0 CB B:VAL200 5.0 32.3 1.0 CD B:GLU128 5.0 36.7 1.0

X.Carpena, B.Wiseman, T.Deemagarn, B.Herguedas, A.Ivancich, R.Singh, P.C.Loewen, I.Fita. Roles For ARG426 and TRP111 in the Modulation of Nadh Oxidase Activity of the Catalase-Peroxidase Katg From Burkholderia Pseudomallei Inferred From pH-Induced Structural Changes. Biochemistry V. 45 5171 2006.
ISSN: ISSN 0006-2960
PubMed: 16618106