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Sodium in PDB 6cc6: Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei

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

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

Protein crystallography data

The structure of Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 6cc6 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) 96.39 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.467, 115.659, 174.421, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 18.1

Other elements in 6cc6:

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

Iron (Fe) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei (pdb code 6cc6). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 6cc6:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 6cc6

Go back to Sodium Binding Sites List in 6cc6
Sodium binding site 1 out of 2 in the Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na802

b:18.4
occ:1.00
O A:GLY124 2.3 18.4 1.0
O A:SER494 2.3 19.2 1.0
O A:GLY122 2.3 17.5 1.0
O A:HOH1221 2.3 19.5 1.0
O A:HOH968 2.4 21.0 1.0
C A:SER494 3.2 17.4 1.0
C A:GLY124 3.4 17.7 1.0
C A:GLY122 3.5 16.6 1.0
C A:ARG123 3.5 16.8 1.0
N A:GLY124 3.5 16.2 1.0
CA A:ARG123 3.6 18.2 1.0
O A:HOH1379 3.9 19.1 1.0
CA A:SER494 4.0 16.6 1.0
N A:ARG123 4.0 16.9 1.0
CA A:GLY124 4.1 17.6 1.0
OD2 A:ASP427 4.1 20.9 1.0
O A:HOH1059 4.1 28.7 1.0
CB A:ASP427 4.1 19.1 1.0
O A:ARG123 4.1 15.9 1.0
N A:ASP495 4.1 17.1 1.0
CB A:SER494 4.2 17.7 1.0
CA A:ASP495 4.4 17.7 1.0
CB A:ASP495 4.5 16.6 1.0
N A:GLY125 4.5 16.0 1.0
CD1 A:TYR117 4.6 19.8 1.0
CG A:ASP427 4.6 21.4 1.0
OE2 A:GLU198 4.7 37.8 1.0
CA A:GLY122 4.8 16.9 1.0
OE2 A:GLU128 4.8 32.1 1.0
OE1 A:GLU198 4.8 23.1 1.0
CE1 A:TYR117 4.9 18.1 1.0
CA A:GLY125 4.9 15.8 1.0
CB A:ARG123 4.9 20.8 1.0
OG A:SER494 5.0 16.1 1.0

Sodium binding site 2 out of 2 in 6cc6

Go back to Sodium Binding Sites List in 6cc6
Sodium binding site 2 out of 2 in the Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na802

b:17.8
occ:1.00
O B:HOH943 2.3 21.6 1.0
O B:GLY122 2.3 15.3 1.0
O B:GLY124 2.3 16.6 1.0
O B:SER494 2.4 20.2 1.0
O B:HOH1014 2.4 22.5 1.0
C B:SER494 3.2 17.6 1.0
C B:GLY122 3.4 16.0 1.0
C B:GLY124 3.5 16.8 1.0
C B:ARG123 3.6 17.3 1.0
N B:GLY124 3.6 17.4 1.0
CA B:ARG123 3.6 17.0 1.0
O B:HOH1288 4.0 20.1 1.0
CA B:SER494 4.0 19.6 1.0
N B:ARG123 4.0 15.2 1.0
O B:HOH1039 4.0 29.8 1.0
OD2 B:ASP427 4.1 20.4 1.0
CA B:GLY124 4.1 17.7 1.0
N B:ASP495 4.1 16.6 1.0
O B:ARG123 4.1 16.4 1.0
CB B:SER494 4.1 19.9 1.0
CB B:ASP427 4.2 18.7 1.0
CA B:ASP495 4.4 16.1 1.0
CB B:ASP495 4.5 15.4 1.0
OE2 B:GLU198 4.6 35.8 1.0
CD1 B:TYR117 4.6 17.1 1.0
N B:GLY125 4.6 14.2 1.0
CG B:ASP427 4.7 18.7 1.0
OE2 B:GLU128 4.7 31.7 1.0
CA B:GLY122 4.7 15.7 1.0
CE1 B:TYR117 4.8 17.1 1.0
CB B:ARG123 4.9 17.1 1.0
OE1 B:GLU198 4.9 23.6 1.0
CA B:GLY125 4.9 15.0 1.0
OG B:SER494 5.0 18.4 1.0

Reference:

P.C.Loewen, P.C.Loewen. N/A N/A.
Page generated: Tue Oct 8 06:34:29 2024

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