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Iron in PDB 5kt8: Crystal Structure of the W139F Variant of the Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid

Enzymatic activity of Crystal Structure of the W139F Variant of the Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid

All present enzymatic activity of Crystal Structure of the W139F Variant of the Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of the W139F Variant of the Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid, PDB code: 5kt8 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) 48.36 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.651, 112.782, 174.539, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 18.6

Other elements in 5kt8:

The structure of Crystal Structure of the W139F Variant of the Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid 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 W139F Variant of the Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid (pdb code 5kt8). 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 W139F Variant of the Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid, PDB code: 5kt8:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5kt8

Go back to Iron Binding Sites List in 5kt8
Iron binding site 1 out of 2 in the Crystal Structure of the W139F Variant of the Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid


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 W139F Variant of the Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:24.7
occ:1.00
 FE A:HEM801 0.0 24.7 1.0
ND A:HEM801 1.9 23.4 1.0
NA A:HEM801 2.0 23.6 1.0
NE2 A:HIS279 2.0 29.9 1.0
NB A:HEM801 2.1 23.9 1.0
NC A:HEM801 2.1 22.3 1.0
O2 A:TOX111 2.6 21.4 0.4
C1D A:HEM801 3.0 24.0 1.0
C4D A:HEM801 3.0 24.2 1.0
C4A A:HEM801 3.0 24.2 1.0
C1A A:HEM801 3.0 23.3 1.0
C4C A:HEM801 3.0 22.1 1.0
C1B A:HEM801 3.0 24.9 1.0
CD2 A:HIS279 3.0 28.3 1.0
CE1 A:HIS279 3.1 27.0 1.0
C4B A:HEM801 3.1 23.6 1.0
C1C A:HEM801 3.2 22.6 1.0
CHD A:HEM801 3.3 22.3 1.0
CHB A:HEM801 3.4 24.6 1.0
CHA A:HEM801 3.4 24.9 1.0
O1 A:TOX111 3.6 23.3 0.6
CHC A:HEM801 3.6 23.6 1.0
ND1 A:HIS279 4.2 27.3 1.0
CG A:HIS279 4.2 26.3 1.0
C3A A:HEM801 4.2 24.9 1.0
C2D A:HEM801 4.2 25.5 1.0
C2A A:HEM801 4.3 25.5 1.0
NE1 A:TOX111 4.3 26.4 1.0
O2 A:TOX111 4.3 22.5 0.2
C3D A:HEM801 4.3 24.5 1.0
C2B A:HEM801 4.3 24.8 1.0
C3B A:HEM801 4.3 24.5 1.0
O1 A:OXY804 4.3 42.8 1.0
C3C A:HEM801 4.3 20.9 1.0
C2C A:HEM801 4.4 21.5 1.0
CD1 A:TOX111 4.5 25.3 1.0

Iron binding site 2 out of 2 in 5kt8

Go back to Iron Binding Sites List in 5kt8
Iron binding site 2 out of 2 in the Crystal Structure of the W139F Variant of the Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid


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 W139F Variant of the Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe801

b:23.0
occ:1.00
 FE B:HEM801 0.0 23.0 1.0
ND B:HEM801 1.9 22.7 1.0
NA B:HEM801 2.0 22.6 1.0
NC B:HEM801 2.0 20.9 1.0
NE2 B:HIS279 2.0 25.4 1.0
NB B:HEM801 2.1 21.9 1.0
O2 B:TOX111 2.8 25.6 0.8
C4D B:HEM801 2.9 21.4 1.0
C1D B:HEM801 3.0 21.8 1.0
CE1 B:HIS279 3.0 27.2 1.0
C4B B:HEM801 3.1 21.6 1.0
C4C B:HEM801 3.1 20.9 1.0
C1A B:HEM801 3.1 23.9 1.0
CD2 B:HIS279 3.1 25.8 1.0
C4A B:HEM801 3.1 23.3 1.0
C1B B:HEM801 3.1 23.3 1.0
C1C B:HEM801 3.1 20.8 1.0
CHD B:HEM801 3.4 21.5 1.0
CHA B:HEM801 3.4 22.3 1.0
CHB B:HEM801 3.5 22.2 1.0
CHC B:HEM801 3.5 20.8 1.0
O1 B:TOX111 3.6 27.7 0.9
ND1 B:HIS279 4.2 25.0 1.0
C2D B:HEM801 4.2 21.2 1.0
C3D B:HEM801 4.2 22.1 1.0
CG B:HIS279 4.2 27.0 1.0
C3A B:HEM801 4.3 22.3 1.0
C3C B:HEM801 4.3 19.8 1.0
C2C B:HEM801 4.3 21.5 1.0
C2A B:HEM801 4.3 21.6 1.0
NE1 B:TOX111 4.3 24.8 1.0
C3B B:HEM801 4.3 22.2 1.0
C2B B:HEM801 4.3 21.6 1.0
O2 B:TOX111 4.4 24.9 0.1
CD1 B:TOX111 4.5 22.9 1.0
O B:HOH976 4.7 41.6 1.0
O1 B:OXY804 4.7 42.3 1.0

Reference:

P.C.Loewen, P.C.Loewen. N/A N/A.
Page generated: Tue Aug 6 03:42:27 2024

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