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Sodium in PDB 5syy: Crystal Structure of the S324G Variant of Catalase-Peroxidase From B. Pseudomallei

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

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

Protein crystallography data

The structure of Crystal Structure of the S324G Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5syy 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 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.909, 113.894, 174.789, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 18.7

Other elements in 5syy:

The structure of Crystal Structure of the S324G Variant of Catalase-Peroxidase From B. Pseudomallei 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 (pdb code 5syy). 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, PDB code: 5syy:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 5syy

Go back to Sodium Binding Sites List in 5syy
Sodium binding site 1 out of 2 in the Crystal Structure of the S324G 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 S324G Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na802

b:19.2
occ:1.00
O A:GLY124 2.3 18.5 1.0
O A:HOH1442 2.4 20.5 1.0
O A:SER494 2.4 18.8 1.0
O A:GLY122 2.4 18.7 1.0
O A:HOH1142 2.4 23.3 1.0
C A:SER494 3.3 19.2 1.0
C A:GLY124 3.5 17.6 1.0
C A:GLY122 3.5 17.7 1.0
N A:GLY124 3.6 18.0 1.0
C A:ARG123 3.6 19.6 1.0
CA A:ARG123 3.6 17.1 1.0
OD2 A:ASP427 4.0 21.9 1.0
N A:ARG123 4.0 17.9 1.0
CA A:SER494 4.0 17.9 1.0
O A:HOH1504 4.1 22.6 1.0
CB A:ASP427 4.1 22.9 1.0
O A:HOH969 4.1 29.1 1.0
N A:ASP495 4.1 18.0 1.0
O A:ARG123 4.1 19.6 1.0
CA A:GLY124 4.1 17.9 1.0
CB A:SER494 4.2 18.6 1.0
CA A:ASP495 4.5 18.5 1.0
CD1 A:TYR117 4.5 18.7 1.0
CB A:ASP495 4.6 17.9 1.0
CG A:ASP427 4.6 25.0 1.0
N A:GLY125 4.6 18.6 1.0
CL A:CL803 4.6 37.8 1.0
CE1 A:TYR117 4.8 19.0 1.0
CA A:GLY122 4.8 19.6 1.0
OE2 A:GLU128 4.8 41.4 1.0
CA A:GLY125 4.9 15.6 1.0
CB A:ARG123 4.9 18.7 1.0

Sodium binding site 2 out of 2 in 5syy

Go back to Sodium Binding Sites List in 5syy
Sodium binding site 2 out of 2 in the Crystal Structure of the S324G 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 S324G Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na802

b:19.6
occ:1.00
O B:GLY122 2.3 17.8 1.0
O B:GLY124 2.3 19.8 1.0
O B:HOH1437 2.3 22.1 1.0
O B:SER494 2.4 20.5 1.0
O B:HOH1035 2.4 24.6 1.0
C B:SER494 3.2 19.6 1.0
C B:GLY122 3.4 17.6 1.0
C B:GLY124 3.5 17.9 1.0
N B:GLY124 3.6 17.9 1.0
C B:ARG123 3.6 18.9 1.0
CA B:ARG123 3.6 17.4 1.0
CA B:SER494 4.0 19.6 1.0
N B:ARG123 4.0 17.9 1.0
O B:HOH1464 4.0 25.2 1.0
OD2 B:ASP427 4.0 25.1 1.0
O B:HOH1179 4.1 32.1 1.0
N B:ASP495 4.1 17.0 1.0
CB B:SER494 4.1 19.3 1.0
O B:ARG123 4.1 17.1 1.0
CA B:GLY124 4.1 18.0 1.0
CB B:ASP427 4.1 23.2 1.0
CA B:ASP495 4.4 18.6 1.0
CB B:ASP495 4.6 18.9 1.0
CD1 B:TYR117 4.6 18.4 1.0
N B:GLY125 4.6 18.0 1.0
CG B:ASP427 4.7 27.5 1.0
CL B:CL803 4.7 36.1 1.0
CA B:GLY122 4.7 18.7 1.0
CE1 B:TYR117 4.8 17.3 1.0
CB B:ARG123 4.9 19.2 1.0
CA B:GLY125 4.9 17.8 1.0
OG B:SER494 5.0 20.5 1.0
O B:HOH1369 5.0 41.8 1.0

Reference:

P.C.Loewen, P.C.Loewen. N/A N/A.
Page generated: Mon Oct 7 23:59:37 2024

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