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Chlorine in PDB 5ksk: Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Acetate

Enzymatic activity of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Acetate

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

Protein crystallography data

The structure of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Acetate, PDB code: 5ksk 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) 48.39 / 1.69
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.703, 115.480, 174.966, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 18

Other elements in 5ksk:

The structure of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Acetate 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 Catalase-Peroxidase From B. Pseudomallei Treated with Acetate (pdb code 5ksk). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Acetate, PDB code: 5ksk:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5ksk

Go back to Chlorine Binding Sites List in 5ksk
Chlorine binding site 1 out of 2 in the Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Acetate


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 Catalase-Peroxidase From B. Pseudomallei Treated with Acetate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl803

b:30.9
occ:1.00
O A:HOH1495 2.9 23.1 1.0
O A:HOH1648 3.0 20.0 1.0
O A:HOH1559 3.1 22.3 1.0
O A:HOH1568 3.2 35.2 1.0
N A:GLY124 3.3 16.5 1.0
CG2 A:VAL200 3.6 24.6 1.0
CB A:GLU198 3.7 32.0 1.0
CG A:GLU198 3.7 36.4 1.0
CA A:GLY124 3.9 17.5 1.0
CB A:ARG123 4.2 20.1 1.0
C A:ARG123 4.3 18.0 1.0
CA A:ARG123 4.4 17.6 1.0
O A:HOH1011 4.4 43.4 1.0
OE1 A:GLU128 4.5 26.8 1.0
NA A:NA802 4.6 19.2 1.0
C A:GLY124 4.6 17.2 1.0
CD A:GLU198 4.6 42.0 1.0
O A:GLY124 4.6 16.6 1.0
CG A:ARG123 4.7 20.1 1.0
O A:HOH1190 4.8 21.5 1.0
CG A:GLN130 4.8 19.0 1.0
CD A:GLU128 5.0 26.9 1.0
CB A:VAL200 5.0 22.6 1.0
OE1 A:GLU198 5.0 40.4 1.0
O A:HOH1054 5.0 17.7 1.0

Chlorine binding site 2 out of 2 in 5ksk

Go back to Chlorine Binding Sites List in 5ksk
Chlorine binding site 2 out of 2 in the Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Acetate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Acetate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl803

b:32.6
occ:1.00
O B:HOH1488 3.1 26.5 1.0
O B:HOH1623 3.1 17.2 1.0
O B:HOH1537 3.2 24.1 1.0
N B:GLY124 3.2 18.2 1.0
O B:HOH1531 3.5 30.5 1.0
CG2 B:VAL200 3.5 21.9 1.0
CG B:GLU198 3.7 37.5 1.0
CB B:GLU198 3.7 32.5 1.0
CA B:GLY124 3.9 17.8 1.0
CB B:ARG123 4.2 17.5 1.0
C B:ARG123 4.3 18.3 1.0
CA B:ARG123 4.3 17.0 1.0
O B:HOH1289 4.4 44.3 1.0
OE1 B:GLU128 4.4 29.3 1.0
CD B:GLU198 4.6 41.4 1.0
C B:GLY124 4.6 17.8 1.0
NA B:NA802 4.7 20.6 1.0
CG B:GLN130 4.7 20.0 1.0
O B:GLY124 4.7 18.3 1.0
CG B:ARG123 4.8 19.8 1.0
O B:HOH1233 4.9 18.5 1.0
OE2 B:GLU128 4.9 34.1 1.0
OE1 B:GLU198 4.9 39.4 1.0
CD B:GLU128 4.9 29.4 1.0
CB B:VAL200 5.0 22.6 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: Sat Dec 12 11:57:27 2020

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