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Chlorine in PDB 6cdq: Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound.

Enzymatic activity of Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound.

All present enzymatic activity of Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound.:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound., PDB code: 6cdq 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) 174.10 / 1.92
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.531, 114.896, 174.099, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 19.9

Other elements in 6cdq:

The structure of Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound. also contains other interesting chemical elements:

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

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound. (pdb code 6cdq). 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 W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound., PDB code: 6cdq:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6cdq

Go back to Chlorine Binding Sites List in 6cdq
Chlorine binding site 1 out of 2 in the Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound.


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 W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl803

b:30.8
occ:1.00
O A:HOH1412 2.9 27.2 1.0
O A:HOH1494 3.0 25.9 1.0
O A:HOH1447 3.3 17.3 1.0
N A:GLY124 3.4 21.0 1.0
N3 A:NIZ809 3.4 20.1 0.5
CG2 A:VAL200 3.5 39.8 1.0
CG A:GLU198 3.5 45.1 1.0
CB A:GLU198 3.7 43.0 1.0
N2 A:NIZ809 4.0 20.7 0.5
CA A:GLY124 4.0 22.1 1.0
CB A:ARG123 4.2 20.4 1.0
CD A:GLU198 4.3 49.8 1.0
CA A:ARG123 4.3 18.7 1.0
C A:ARG123 4.3 20.4 1.0
OE1 A:GLU128 4.6 28.6 1.0
OE2 A:GLU198 4.6 45.1 1.0
NA A:NA802 4.7 20.5 1.0
CG A:ARG123 4.7 21.0 1.0
O A:GLY124 4.8 19.3 1.0
OE2 A:GLU128 4.8 33.0 1.0
CB A:VAL200 4.8 35.2 1.0
C A:GLY124 4.8 20.9 1.0
O A:HOH1404 4.8 23.4 1.0
C A:NIZ809 4.9 22.7 0.5
CD A:GLU128 4.9 32.0 1.0
CG1 A:VAL200 4.9 36.2 1.0
CG A:GLN130 5.0 17.8 1.0
OE1 A:GLU198 5.0 50.2 1.0

Chlorine binding site 2 out of 2 in 6cdq

Go back to Chlorine Binding Sites List in 6cdq
Chlorine binding site 2 out of 2 in the Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound.


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 W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl803

b:27.5
occ:1.00
O B:HOH1487 3.0 18.7 1.0
O B:HOH1355 3.2 24.1 1.0
O B:HOH1437 3.2 22.6 1.0
N B:GLY124 3.3 20.9 1.0
CG2 B:VAL200 3.3 36.5 1.0
CG B:GLU198 3.5 38.3 1.0
N3 B:NIZ808 3.6 31.6 1.0
CB B:GLU198 3.7 35.5 1.0
N2 B:NIZ808 3.9 36.8 1.0
CA B:GLY124 4.0 19.9 1.0
CB B:ARG123 4.2 18.1 1.0
CD B:GLU198 4.3 39.7 1.0
C B:ARG123 4.3 21.4 1.0
CA B:ARG123 4.3 19.5 1.0
OE1 B:GLU128 4.6 28.4 1.0
OE2 B:GLU198 4.6 36.4 1.0
OE2 B:GLU128 4.6 32.8 1.0
CG B:ARG123 4.7 20.0 1.0
CB B:VAL200 4.7 33.9 1.0
O B:HOH1412 4.7 27.5 1.0
C B:GLY124 4.7 18.5 1.0
NA B:NA802 4.7 19.3 1.0
O B:GLY124 4.8 17.8 1.0
CD B:GLU128 4.9 28.6 1.0
CG B:GLN130 4.9 17.7 1.0
OE1 B:GLU198 5.0 48.8 1.0
CG1 B:VAL200 5.0 37.1 1.0
O B:HOH1143 5.0 17.9 1.0

Reference:

P.C.Loewen, P.C.Loewen. N/A N/A.
Page generated: Sat Jul 12 12:22:18 2025

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