Atomistry » Sodium » PDB 6awz-6bfo » 6b9b
Atomistry »
  Sodium »
    PDB 6awz-6bfo »
      6b9b »

Sodium in PDB 6b9b: Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose Bound

Enzymatic activity of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose Bound

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

Protein crystallography data

The structure of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose Bound, PDB code: 6b9b 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) 50.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.419, 115.088, 174.975, 90.00, 90.00, 90.00
R / Rfree (%) 13.5 / 16.2

Other elements in 6b9b:

The structure of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose 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 Catalase-Peroxidase From B. Pseudomallei with Maltose Bound (pdb code 6b9b). 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 Catalase-Peroxidase From B. Pseudomallei with Maltose Bound, PDB code: 6b9b:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 6b9b

Go back to Sodium Binding Sites List in 6b9b
Sodium binding site 1 out of 2 in the Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose 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 Catalase-Peroxidase From B. Pseudomallei with Maltose Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na802

b:19.3
occ:1.00
O A:GLY124 2.3 17.2 1.0
O A:HOH1066 2.4 21.6 1.0
O A:SER494 2.4 18.5 1.0
O A:HOH1450 2.4 20.3 1.0
O A:GLY122 2.4 18.8 1.0
C A:SER494 3.2 19.1 1.0
C A:GLY124 3.5 18.3 1.0
C A:GLY122 3.6 18.4 1.0
N A:GLY124 3.6 17.0 1.0
CA A:ARG123 3.6 18.5 1.0
C A:ARG123 3.6 17.5 1.0
O A:HOH1488 3.9 21.1 1.0
CA A:SER494 3.9 17.3 1.0
O A:HOH1024 4.0 29.4 1.0
OD2 A:ASP427 4.0 18.7 1.0
N A:ARG123 4.1 17.3 1.0
N A:ASP495 4.1 16.3 1.0
CB A:ASP427 4.1 20.7 1.0
O A:ARG123 4.1 16.4 1.0
CA A:GLY124 4.1 18.4 1.0
CB A:SER494 4.1 19.4 1.0
CA A:ASP495 4.4 18.9 1.0
N A:GLY125 4.6 17.5 1.0
CG A:ASP427 4.6 21.9 1.0
CB A:ASP495 4.6 16.9 1.0
CL A:CL803 4.6 36.2 1.0
CD1 A:TYR117 4.6 20.0 1.0
O A:HOH1145 4.8 43.5 1.0
CA A:GLY122 4.8 17.8 1.0
CA A:GLY125 4.9 17.4 1.0
CE1 A:TYR117 4.9 19.6 1.0
CB A:ARG123 4.9 18.9 1.0
OE2 A:GLU128 5.0 31.2 1.0
OG A:SER494 5.0 18.4 1.0

Sodium binding site 2 out of 2 in 6b9b

Go back to Sodium Binding Sites List in 6b9b
Sodium binding site 2 out of 2 in the Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose 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 Catalase-Peroxidase From B. Pseudomallei with Maltose Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na802

b:19.6
occ:1.00
O B:HOH1474 2.3 24.2 1.0
O B:GLY124 2.4 17.2 1.0
O B:GLY122 2.4 16.8 1.0
O B:HOH1068 2.4 21.8 1.0
O B:SER494 2.4 18.3 1.0
C B:SER494 3.2 18.7 1.0
C B:GLY122 3.5 17.3 1.0
C B:GLY124 3.5 18.0 1.0
C B:ARG123 3.6 16.4 1.0
N B:GLY124 3.6 18.9 1.0
CA B:ARG123 3.6 17.2 1.0
CA B:SER494 4.0 17.6 1.0
O B:HOH1518 4.0 20.1 1.0
N B:ARG123 4.0 15.7 1.0
O B:HOH1016 4.0 30.1 1.0
N B:ASP495 4.1 18.0 1.0
CB B:SER494 4.1 18.0 1.0
O B:ARG123 4.1 16.5 1.0
OD2 B:ASP427 4.1 20.3 1.0
CB B:ASP427 4.2 20.1 1.0
CA B:GLY124 4.2 17.0 1.0
CA B:ASP495 4.5 16.8 1.0
CB B:ASP495 4.6 17.2 1.0
CD1 B:TYR117 4.6 17.0 1.0
N B:GLY125 4.6 15.9 1.0
CG B:ASP427 4.7 19.1 1.0
CL B:CL803 4.7 38.2 1.0
CA B:GLY122 4.8 17.5 1.0
CE1 B:TYR117 4.9 18.4 1.0
CA B:GLY125 4.9 16.3 1.0
CB B:ARG123 4.9 16.2 1.0
OE2 B:GLU128 4.9 31.4 1.0
OG B:SER494 5.0 17.4 1.0

Reference:

P.C.Loewen, P.M.De Silva, L.J.Donald, J.Switala, J.Villanueva, I.Fita, A.Kumar. Katg-Mediated Oxidation Leading to Reduced Susceptibility of Bacteria to Kanamycin. Acs Omega V. 3 4213 2018.
ISSN: ESSN 2470-1343
PubMed: 29732452
DOI: 10.1021/ACSOMEGA.8B00356
Page generated: Tue Oct 8 01:59:50 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy