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Iron in PDB 5sx7: Crystal Structure of Catalase-Peroxidase Katg of B. Pseudomallei at pH 8.5

Enzymatic activity of Crystal Structure of Catalase-Peroxidase Katg of B. Pseudomallei at pH 8.5

All present enzymatic activity of Crystal Structure of Catalase-Peroxidase Katg of B. Pseudomallei at pH 8.5:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of Catalase-Peroxidase Katg of B. Pseudomallei at pH 8.5, PDB code: 5sx7 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 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.413, 114.948, 173.998, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 18.9

Other elements in 5sx7:

The structure of Crystal Structure of Catalase-Peroxidase Katg of B. Pseudomallei at pH 8.5 also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Catalase-Peroxidase Katg of B. Pseudomallei at pH 8.5 (pdb code 5sx7). 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 Catalase-Peroxidase Katg of B. Pseudomallei at pH 8.5, PDB code: 5sx7:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5sx7

Go back to Iron Binding Sites List in 5sx7
Iron binding site 1 out of 2 in the Crystal Structure of Catalase-Peroxidase Katg of B. Pseudomallei at pH 8.5


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 Catalase-Peroxidase Katg of B. Pseudomallei at pH 8.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:16.6
occ:1.00
FE A:HEM801 0.0 16.6 1.0
ND A:HEM801 1.9 15.7 1.0
NA A:HEM801 2.0 15.5 1.0
NE2 A:HIS279 2.1 18.0 1.0
NC A:HEM801 2.1 15.6 1.0
NB A:HEM801 2.1 16.0 1.0
O2 A:TOX111 2.5 21.5 0.7
C4D A:HEM801 3.0 15.8 1.0
C1D A:HEM801 3.0 15.4 1.0
C4A A:HEM801 3.0 15.6 1.0
C4C A:HEM801 3.0 15.6 1.0
CD2 A:HIS279 3.0 16.8 1.0
C1B A:HEM801 3.1 16.5 1.0
C1C A:HEM801 3.1 15.3 1.0
CE1 A:HIS279 3.1 17.4 1.0
C1A A:HEM801 3.1 15.4 1.0
C4B A:HEM801 3.1 16.2 1.0
CHD A:HEM801 3.4 15.6 1.0
CHB A:HEM801 3.4 16.6 1.0
CHA A:HEM801 3.4 15.4 1.0
CHC A:HEM801 3.5 14.8 1.0
O1 A:TOX111 3.6 22.3 0.8
O1 A:OXY803 3.9 36.4 1.0
ND1 A:HIS279 4.2 17.3 1.0
CG A:HIS279 4.2 16.8 1.0
C2D A:HEM801 4.2 15.6 1.0
C3A A:HEM801 4.3 15.1 1.0
NE1 A:TOX111 4.3 17.2 1.0
C3D A:HEM801 4.3 16.2 1.0
C2B A:HEM801 4.3 16.2 1.0
C2C A:HEM801 4.3 14.8 1.0
C3C A:HEM801 4.3 14.9 1.0
C2A A:HEM801 4.3 15.5 1.0
C3B A:HEM801 4.4 15.2 1.0
CD1 A:TOX111 4.4 16.5 1.0
O2 A:TOX111 4.5 19.1 0.1
O2 A:OXY803 4.9 30.6 1.0
O A:HOH905 5.0 38.9 1.0

Iron binding site 2 out of 2 in 5sx7

Go back to Iron Binding Sites List in 5sx7
Iron binding site 2 out of 2 in the Crystal Structure of Catalase-Peroxidase Katg of B. Pseudomallei at pH 8.5


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 Catalase-Peroxidase Katg of B. Pseudomallei at pH 8.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe802

b:14.4
occ:1.00
FE B:HEM802 0.0 14.4 1.0
ND B:HEM802 2.0 14.2 1.0
NA B:HEM802 2.0 13.8 1.0
NC B:HEM802 2.0 14.5 1.0
NE2 B:HIS279 2.0 15.7 1.0
NB B:HEM802 2.1 13.7 1.0
O2 B:TOX111 2.5 28.8 1.0
C4D B:HEM802 3.0 13.5 1.0
C1D B:HEM802 3.0 14.1 1.0
C4A B:HEM802 3.0 14.0 1.0
C4B B:HEM802 3.0 13.8 1.0
CD2 B:HIS279 3.0 15.6 1.0
C1B B:HEM802 3.1 14.0 1.0
C1A B:HEM802 3.1 13.1 1.0
CE1 B:HIS279 3.1 15.4 1.0
C4C B:HEM802 3.1 14.3 1.0
C1C B:HEM802 3.1 14.2 1.0
CHD B:HEM802 3.4 13.9 1.0
CHB B:HEM802 3.4 13.7 1.0
CHA B:HEM802 3.4 13.4 1.0
CHC B:HEM802 3.4 13.6 1.0
O1 B:TOX111 3.6 25.6 1.0
ND1 B:HIS279 4.2 15.2 1.0
C3D B:HEM802 4.2 14.6 1.0
C2D B:HEM802 4.2 14.5 1.0
CG B:HIS279 4.2 14.9 1.0
O1 B:OXY804 4.2 27.1 1.0
C3A B:HEM802 4.2 14.4 1.0
C2A B:HEM802 4.2 14.1 1.0
C2B B:HEM802 4.2 13.3 1.0
C3B B:HEM802 4.3 13.8 1.0
NE1 B:TOX111 4.3 18.0 1.0
C3C B:HEM802 4.3 14.4 1.0
C2C B:HEM802 4.3 13.8 1.0
CD1 B:TOX111 4.5 16.0 1.0

Reference:

X.Carpena, B.Wiseman, T.Deemagarn, B.Herguedas, A.Ivancich, R.Singh, P.C.Loewen, I.Fita. Roles For ARG426 and TRP111 in the Modulation of Nadh Oxidase Activity of the Catalase-Peroxidase Katg From Burkholderia Pseudomallei Inferred From pH-Induced Structural Changes. Biochemistry V. 45 5171 2006.
ISSN: ISSN 0006-2960
PubMed: 16618106
Page generated: Wed Aug 6 01:25:18 2025

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