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Sodium in PDB 5ksn: Crystal Structure of the S324G Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound

Enzymatic activity of Crystal Structure of the S324G Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound

All present enzymatic activity of Crystal Structure of the S324G Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of the S324G Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound, PDB code: 5ksn 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) 48.05 / 1.87
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.434, 115.277, 174.118, 90.00, 90.00, 90.00
R / Rfree (%) 14.2 / 17.1

Other elements in 5ksn:

The structure of Crystal Structure of the S324G Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound also contains other interesting chemical elements:

Iron (Fe) 2 atoms
Chlorine (Cl) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the S324G Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound (pdb code 5ksn). 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 S324G Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound, PDB code: 5ksn:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 5ksn

Go back to Sodium Binding Sites List in 5ksn
Sodium binding site 1 out of 2 in the Crystal Structure of the S324G Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound


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 S324G Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na802

b:15.3
occ:1.00
O A:HOH1080 2.3 15.9 1.0
O A:GLY124 2.3 14.8 1.0
O A:SER494 2.3 15.6 1.0
O A:HOH1468 2.4 16.7 1.0
O A:GLY122 2.4 14.8 1.0
C A:SER494 3.2 14.5 1.0
C A:GLY124 3.5 13.8 1.0
C A:GLY122 3.5 13.8 1.0
C A:ARG123 3.6 13.9 1.0
CA A:ARG123 3.6 13.8 1.0
N A:GLY124 3.6 13.6 1.0
O A:HOH1557 3.9 17.2 1.0
CA A:SER494 4.0 14.8 1.0
OD2 A:ASP427 4.0 13.8 1.0
N A:ARG123 4.1 13.7 1.0
N A:ASP495 4.1 14.7 1.0
CA A:GLY124 4.1 14.9 1.0
CB A:ASP427 4.1 14.1 1.0
O A:HOH977 4.1 27.0 1.0
O A:ARG123 4.2 13.6 1.0
CB A:SER494 4.2 14.8 1.0
CA A:ASP495 4.4 14.5 1.0
CL A:CL803 4.5 25.9 1.0
N A:GLY125 4.6 13.3 1.0
CB A:ASP495 4.6 14.7 1.0
CG A:ASP427 4.6 14.2 1.0
CD1 A:TYR117 4.7 15.4 1.0
CA A:GLY122 4.8 14.0 1.0
OE2 A:GLU128 4.8 24.4 1.0
CA A:GLY125 4.8 12.5 1.0
CB A:ARG123 4.9 14.9 1.0

Sodium binding site 2 out of 2 in 5ksn

Go back to Sodium Binding Sites List in 5ksn
Sodium binding site 2 out of 2 in the Crystal Structure of the S324G Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound


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 S324G Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na802

b:14.9
occ:1.00
O B:HOH1468 2.3 14.3 1.0
O B:SER494 2.3 13.0 1.0
O B:GLY124 2.3 13.3 1.0
O B:GLY122 2.4 12.1 1.0
O B:HOH1050 2.4 17.7 1.0
C B:SER494 3.1 13.8 1.0
C B:GLY122 3.5 12.8 1.0
C B:GLY124 3.5 12.0 1.0
N B:GLY124 3.6 13.3 1.0
C B:ARG123 3.6 13.6 1.0
CA B:ARG123 3.6 13.2 1.0
CA B:SER494 3.9 13.8 1.0
OD2 B:ASP427 4.0 15.0 1.0
O B:HOH1599 4.0 15.4 1.0
N B:ASP495 4.0 13.3 1.0
N B:ARG123 4.1 12.8 1.0
CB B:SER494 4.1 13.9 1.0
O B:HOH1090 4.1 21.2 1.0
CA B:GLY124 4.2 12.7 1.0
CB B:ASP427 4.2 16.6 1.0
O B:ARG123 4.2 13.9 1.0
CA B:ASP495 4.4 12.9 1.0
CB B:ASP495 4.5 12.6 1.0
CG B:ASP427 4.6 14.6 1.0
N B:GLY125 4.6 12.1 1.0
CL B:CL803 4.6 23.4 1.0
OE2 B:GLU128 4.7 24.1 1.0
CD1 B:TYR117 4.7 14.4 1.0
CA B:GLY122 4.8 12.6 1.0
CB B:ARG123 4.9 12.9 1.0
CA B:GLY125 4.9 12.4 1.0
OG B:SER494 4.9 14.6 1.0

Reference:

P.C.Loewen, P.C.Loewen. N/A N/A.
Page generated: Mon Aug 18 00:43:05 2025

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