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Iron in PDB 5kt9: Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Hydrogen Peroxide and Carbon Monoxide

Enzymatic activity of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Hydrogen Peroxide and Carbon Monoxide

All present enzymatic activity of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Hydrogen Peroxide and Carbon Monoxide:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Hydrogen Peroxide and Carbon Monoxide, PDB code: 5kt9 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 / 1.88
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.854, 113.790, 174.633, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 21.3

Other elements in 5kt9:

The structure of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Hydrogen Peroxide and Carbon Monoxide also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Sodium (Na) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Hydrogen Peroxide and Carbon Monoxide (pdb code 5kt9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Hydrogen Peroxide and Carbon Monoxide, PDB code: 5kt9:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5kt9

Go back to Iron Binding Sites List in 5kt9
Iron binding site 1 out of 2 in the Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Hydrogen Peroxide and Carbon Monoxide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Hydrogen Peroxide and Carbon Monoxide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:20.1
occ:1.00
 FE A:HEM801 0.0 20.1 1.0
ND A:HEM801 2.0 20.1 1.0
NA A:HEM801 2.1 20.9 1.0
NC A:HEM801 2.1 19.3 1.0
NB A:HEM801 2.1 19.5 1.0
NE2 A:HIS279 2.1 21.0 1.0
O2 A:TOX111 2.5 26.7 0.6
C1D A:HEM801 2.9 18.4 1.0
C4D A:HEM801 3.0 19.8 1.0
C4C A:HEM801 3.0 19.9 1.0
C1A A:HEM801 3.1 21.2 1.0
C4B A:HEM801 3.1 19.8 1.0
C4A A:HEM801 3.1 22.2 1.0
C1C A:HEM801 3.1 19.9 1.0
C1B A:HEM801 3.1 21.1 1.0
CE1 A:HIS279 3.1 20.3 1.0
CD2 A:HIS279 3.1 19.5 1.0
CHD A:HEM801 3.3 18.1 1.0
CHA A:HEM801 3.4 21.8 1.0
CHC A:HEM801 3.5 18.9 1.0
CHB A:HEM801 3.5 19.6 1.0
O1 A:TOX111 3.5 27.8 0.8
C2D A:HEM801 4.2 19.5 1.0
NE1 A:TOX111 4.2 21.9 1.0
C3D A:HEM801 4.2 20.0 1.0
C3C A:HEM801 4.3 19.4 1.0
ND1 A:HIS279 4.3 19.1 1.0
O2 A:TOX111 4.3 23.1 0.2
C3A A:HEM801 4.3 22.6 1.0
CG A:HIS279 4.3 20.0 1.0
C2A A:HEM801 4.3 23.2 1.0
C2C A:HEM801 4.3 19.3 1.0
C3B A:HEM801 4.3 19.8 1.0
C2B A:HEM801 4.4 20.5 1.0
CD1 A:TOX111 4.5 22.4 1.0
O2 A:OXY804 4.6 37.1 1.0
O A:HOH1042 5.0 46.2 1.0

Iron binding site 2 out of 2 in 5kt9

Go back to Iron Binding Sites List in 5kt9
Iron binding site 2 out of 2 in the Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Hydrogen Peroxide and Carbon Monoxide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei Treated with Hydrogen Peroxide and Carbon Monoxide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe801

b:21.4
occ:1.00
 FE B:HEM801 0.0 21.4 1.0
ND B:HEM801 1.9 20.8 1.0
NC B:HEM801 2.0 18.5 1.0
NA B:HEM801 2.1 17.8 1.0
NB B:HEM801 2.1 21.1 1.0
NE2 B:HIS279 2.1 24.9 1.0
O2 B:TOX111 2.9 26.2 0.6
C4D B:HEM801 3.0 19.6 1.0
C4C B:HEM801 3.0 20.1 1.0
C1D B:HEM801 3.0 19.3 1.0
C1A B:HEM801 3.0 20.9 1.0
C4B B:HEM801 3.0 21.2 1.0
C1C B:HEM801 3.0 18.8 1.0
C4A B:HEM801 3.0 19.9 1.0
CD2 B:HIS279 3.1 23.1 1.0
CE1 B:HIS279 3.1 21.8 1.0
C1B B:HEM801 3.1 21.2 1.0
CHC B:HEM801 3.4 21.5 1.0
CHD B:HEM801 3.4 19.5 1.0
CHA B:HEM801 3.4 20.9 1.0
CHB B:HEM801 3.5 19.9 1.0
O1 B:TOX111 3.5 26.6 1.0
C2D B:HEM801 4.2 20.9 1.0
C3D B:HEM801 4.2 21.2 1.0
NE1 B:TOX111 4.2 21.7 1.0
ND1 B:HIS279 4.2 22.7 1.0
C2C B:HEM801 4.3 18.4 1.0
C3C B:HEM801 4.3 18.6 1.0
CG B:HIS279 4.3 24.3 1.0
C3B B:HEM801 4.3 21.5 1.0
O2 B:TOX111 4.3 23.8 0.4
C3A B:HEM801 4.3 18.5 1.0
C2A B:HEM801 4.3 18.8 1.0
C2B B:HEM801 4.3 22.2 1.0
O2 B:OXY805 4.5 42.8 1.0
CD1 B:TOX111 4.6 21.3 1.0
O B:HOH949 4.8 40.6 1.0

Reference:

P.C.Loewen, P.C.Loewen. N/A N/A.
Page generated: Tue Aug 6 03:42:29 2024

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