Atomistry » Chlorine » PDB 5kq0-5kvy » 5kqh
Atomistry »
  Chlorine »
    PDB 5kq0-5kvy »
      5kqh »

Chlorine in PDB 5kqh: Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei

Enzymatic activity of Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei

All present enzymatic activity of Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kqh 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) 47.56 / 1.82
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.787, 113.434, 174.677, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 18.4

Other elements in 5kqh:

The structure of Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei also contains other interesting chemical elements:

Iron (Fe) 2 atoms
Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei (pdb code 5kqh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kqh:

Chlorine binding site 1 out of 1 in 5kqh

Go back to Chlorine Binding Sites List in 5kqh
Chlorine binding site 1 out of 1 in the Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the V293D Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl803

b:32.9
occ:1.00
 O A:HOH1483 3.0 19.2 1.0
O A:HOH1544 3.0 20.6 1.0
O A:HOH1627 3.0 16.3 1.0
N A:GLY124 3.3 14.6 1.0
CG A:GLU198 3.4 43.1 1.0
CB A:GLU198 3.4 34.6 1.0
CG2 A:VAL200 3.6 22.6 1.0
CA A:GLY124 3.9 14.8 1.0
CB A:ARG123 4.3 14.2 1.0
OE1 A:GLU128 4.3 26.0 1.0
C A:ARG123 4.4 15.3 1.0
CA A:ARG123 4.4 13.9 1.0
CD A:GLU198 4.5 47.6 1.0
O A:HOH1098 4.6 45.0 1.0
CG A:GLN130 4.7 15.9 1.0
NA A:NA802 4.7 15.8 1.0
C A:GLY124 4.7 14.5 1.0
O A:GLY124 4.7 16.1 1.0
O A:HOH1264 4.8 17.3 1.0
OE2 A:GLU128 4.8 34.3 1.0
CD A:GLU128 4.8 26.8 1.0
CG A:ARG123 4.9 13.2 1.0
OE2 A:GLU198 4.9 46.3 1.0
CA A:GLU198 5.0 27.4 1.0
O A:HOH1314 5.0 15.7 1.0

Reference:

M.Machuqueiro, B.Victor, J.Switala, J.Villanueva, C.Rovira, I.Fita, P.C.Loewen. The Catalase Activity of Catalase-Peroxidases Is Modulated By Changes in the Pka of the Distal Histidine. Biochemistry V. 56 2271 2017.
ISSN: ISSN 1520-4995
PubMed: 28409923
DOI: 10.1021/ACS.BIOCHEM.6B01276
Page generated: Fri Jul 26 10:48:43 2024

Last articles

Cl in 2VR4
Cl in 2VTJ
Cl in 2VTR
Cl in 2VT7
Cl in 2VT6
Cl in 2VSY
Cl in 2VQT
Cl in 2VRS
Cl in 2VRP
Cl in 2VRE
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy