Atomistry » Sodium » PDB 5rdn-5syl » 5sxx
Atomistry »
  Sodium »
    PDB 5rdn-5syl »
      5sxx »

Sodium in PDB 5sxx: Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh

Enzymatic activity of Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh

All present enzymatic activity of Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh, PDB code: 5sxx 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 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.570, 115.940, 174.730, 90.00, 90.00, 90.00
R / Rfree (%) 14.2 / 16.9

Other elements in 5sxx:

The structure of Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh 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 E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh (pdb code 5sxx). 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 E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh, PDB code: 5sxx:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 5sxx

Go back to Sodium Binding Sites List in 5sxx
Sodium binding site 1 out of 2 in the Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh


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 E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na802

b:17.8
occ:1.00
O A:GLY124 2.4 13.9 1.0
O A:SER494 2.4 17.7 1.0
O A:HOH992 2.4 22.6 1.0
O A:GLY122 2.4 13.7 1.0
O A:HOH1533 2.5 22.0 1.0
C A:SER494 3.2 14.9 1.0
N A:GLY124 3.5 13.3 1.0
C A:GLY122 3.5 13.9 1.0
C A:GLY124 3.5 13.3 1.0
CA A:ARG123 3.5 14.3 1.0
C A:ARG123 3.6 12.9 1.0
O A:HOH1025 3.9 38.5 1.0
O A:HOH1528 3.9 24.1 1.0
CA A:SER494 3.9 13.0 1.0
N A:ARG123 4.0 12.8 1.0
OD2 A:ASP427 4.0 17.0 1.0
N A:ASP495 4.1 13.3 1.0
CB A:SER494 4.1 13.2 1.0
CA A:GLY124 4.1 12.9 1.0
CB A:ASP427 4.2 16.1 1.0
O A:ARG123 4.2 13.2 1.0
CL A:CL803 4.4 62.0 1.0
CA A:ASP495 4.5 13.9 1.0
CB A:ASP495 4.6 13.9 1.0
N A:GLY125 4.6 11.9 1.0
CG A:ASP427 4.6 16.7 1.0
CD1 A:TYR117 4.7 13.3 1.0
CB A:ARG123 4.8 14.2 1.0
CA A:GLY122 4.8 12.8 1.0
CA A:GLY125 4.9 11.2 1.0
CE1 A:TYR117 5.0 13.7 1.0
OG A:SER494 5.0 12.9 1.0

Sodium binding site 2 out of 2 in 5sxx

Go back to Sodium Binding Sites List in 5sxx
Sodium binding site 2 out of 2 in the Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh


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 E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na802

b:19.4
occ:1.00
O B:HOH1520 2.3 29.7 1.0
O B:SER494 2.4 18.9 1.0
O B:GLY124 2.5 13.6 1.0
O B:GLY122 2.5 12.3 1.0
O B:HOH933 2.5 24.7 1.0
C B:SER494 3.3 17.6 1.0
N B:GLY124 3.5 12.9 1.0
C B:ARG123 3.6 12.3 1.0
C B:GLY122 3.6 11.9 1.0
CA B:ARG123 3.6 13.2 1.0
C B:GLY124 3.6 13.8 1.0
O B:HOH1069 3.9 38.4 1.0
CA B:SER494 3.9 13.8 1.0
O B:HOH1553 3.9 23.3 1.0
N B:ARG123 4.1 11.8 1.0
OD2 B:ASP427 4.1 17.3 1.0
CB B:SER494 4.1 14.3 1.0
N B:ASP495 4.1 13.9 1.0
CA B:GLY124 4.2 12.7 1.0
O B:ARG123 4.2 12.5 1.0
CL B:CL803 4.3 54.1 1.0
CB B:ASP427 4.3 17.0 1.0
CA B:ASP495 4.5 13.4 1.0
CB B:ASP495 4.7 14.2 1.0
CG B:ASP427 4.7 17.8 1.0
N B:GLY125 4.7 12.4 1.0
CB B:ARG123 4.8 12.4 1.0
CD1 B:TYR117 4.8 13.8 1.0
CA B:GLY122 4.9 11.4 1.0
OG B:SER494 5.0 15.0 1.0

Reference:

B.Wiseman, X.Carpena, M.Feliz, L.J.Donald, M.Pons, I.Fita, P.C.Loewen. Isonicotinic Acid Hydrazide Conversion to Isonicotinyl-Nad By Catalase-Peroxidases. J. Biol. Chem. V. 285 26662 2010.
ISSN: ESSN 1083-351X
PubMed: 20554537
DOI: 10.1074/JBC.M110.139428
Page generated: Mon Oct 7 23:58:03 2024

Last articles

Mg in 4GMJ
Mg in 4GNK
Mg in 4GNI
Mg in 4GN0
Mg in 4GMX
Mg in 4GME
Mg in 4GKM
Mg in 4GKR
Mg in 4GHL
Mg in 4GIU
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy