Iron in PDB 5sx6: Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomallei at pH 6.5

All present enzymatic activity of Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomallei at pH 6.5:
1.11.1.21;

The structure of Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomallei at pH 6.5, PDB code: 5sx6 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 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.529, 114.795, 174.647, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 17.2

The structure of Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomallei at pH 6.5 also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Iron atom in the Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomallei at pH 6.5 (pdb code 5sx6). 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 Katg of B. Pseudomallei at pH 6.5, PDB code: 5sx6:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomallei at pH 6.5


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 the Catalase-Peroxidase Katg of B. Pseudomallei at pH 6.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:19.7 occ:1.00 FE A:HEM801 0.0 19.7 1.0 ND A:HEM801 2.0 19.9 1.0 NA A:HEM801 2.1 20.0 1.0 NC A:HEM801 2.1 20.5 1.0 NE2 A:HIS279 2.1 23.4 1.0 NB A:HEM801 2.1 20.6 1.0 O2 A:TOX111 2.7 23.9 0.4 C4D A:HEM801 3.0 19.3 1.0 C1D A:HEM801 3.0 19.8 1.0 C4C A:HEM801 3.0 19.2 1.0 C1C A:HEM801 3.1 18.7 1.0 CE1 A:HIS279 3.1 21.3 1.0 C4A A:HEM801 3.1 19.1 1.0 C1A A:HEM801 3.1 19.6 1.0 C1B A:HEM801 3.1 21.0 1.0 CD2 A:HIS279 3.1 20.6 1.0 C4B A:HEM801 3.1 21.4 1.0 CHD A:HEM801 3.4 18.7 1.0 CHA A:HEM801 3.4 21.0 1.0 CHC A:HEM801 3.5 19.1 1.0 O1 A:TOX111 3.5 25.6 0.5 CHB A:HEM801 3.5 22.0 1.0 O2 A:TOX111 4.1 21.2 0.1 O1 A:OXY803 4.2 45.3 1.0 ND1 A:HIS279 4.2 20.8 1.0 C3D A:HEM801 4.2 20.3 1.0 CG A:HIS279 4.2 21.5 1.0 C2D A:HEM801 4.3 18.3 1.0 C2B A:HEM801 4.3 23.1 1.0 C2A A:HEM801 4.3 21.0 1.0 C3A A:HEM801 4.3 20.8 1.0 C2C A:HEM801 4.3 18.5 1.0 NE1 A:TOX111 4.3 20.9 1.0 C3C A:HEM801 4.3 18.7 1.0 C3B A:HEM801 4.3 20.1 1.0 CD1 A:TOX111 4.5 21.6 1.0 O A:HOH905 4.9 55.5 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Catalase-Peroxidase Katg of B. Pseudomallei at pH 6.5


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 the Catalase-Peroxidase Katg of B. Pseudomallei at pH 6.5 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:16.1 occ:1.00 FE B:HEM801 0.0 16.1 1.0 ND B:HEM801 2.0 15.0 1.0 NA B:HEM801 2.0 15.5 1.0 NE2 B:HIS279 2.0 17.8 1.0 NC B:HEM801 2.1 14.9 1.0 NB B:HEM801 2.1 16.0 1.0 O2 B:TOX111 2.6 18.4 0.5 C1A B:HEM801 2.9 16.1 1.0 C4A B:HEM801 3.0 17.1 1.0 C4B B:HEM801 3.0 15.7 1.0 C1C B:HEM801 3.0 14.6 1.0 C4D B:HEM801 3.0 15.1 1.0 C1D B:HEM801 3.0 14.6 1.0 CE1 B:HIS279 3.1 16.9 1.0 C4C B:HEM801 3.1 14.2 1.0 CD2 B:HIS279 3.1 17.6 1.0 C1B B:HEM801 3.1 16.4 1.0 CHA B:HEM801 3.3 15.6 1.0 CHC B:HEM801 3.4 15.5 1.0 CHB B:HEM801 3.4 16.4 1.0 CHD B:HEM801 3.4 15.2 1.0 O1 B:TOX111 3.6 20.9 0.6 ND1 B:HIS279 4.2 17.5 1.0 C2A B:HEM801 4.2 15.1 1.0 C2D B:HEM801 4.2 14.6 1.0 C3D B:HEM801 4.2 15.1 1.0 C3A B:HEM801 4.2 16.3 1.0 CG B:HIS279 4.3 17.3 1.0 C3B B:HEM801 4.3 16.5 1.0 NE1 B:TOX111 4.3 17.8 1.0 C3C B:HEM801 4.3 15.0 1.0 C2C B:HEM801 4.3 14.2 1.0 C2B B:HEM801 4.3 16.0 1.0 O2 B:TOX111 4.3 17.2 0.1 CD1 B:TOX111 4.5 18.0 1.0 O1 B:OXY803 4.6 31.9 1.0

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