Iron in PDB 5syu: Crystal Structure of Burkholderia Pseudomallei Katg E242Q Variant

All present enzymatic activity of Crystal Structure of Burkholderia Pseudomallei Katg E242Q Variant:
1.11.1.21;

The structure of Crystal Structure of Burkholderia Pseudomallei Katg E242Q Variant, PDB code: 5syu 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)	47.65 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.997, 113.675, 174.786, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 17.3

The structure of Crystal Structure of Burkholderia Pseudomallei Katg E242Q Variant also contains other interesting chemical elements:

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

The binding sites of Iron atom in the Crystal Structure of Burkholderia Pseudomallei Katg E242Q Variant (pdb code 5syu). 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 Burkholderia Pseudomallei Katg E242Q Variant, PDB code: 5syu:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Burkholderia Pseudomallei Katg E242Q Variant


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 Burkholderia Pseudomallei Katg E242Q Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:14.4 occ:1.00 FE A:HEM801 0.0 14.4 1.0 ND A:HEM801 2.0 12.9 1.0 NA A:HEM801 2.0 14.9 1.0 NC A:HEM801 2.0 14.6 1.0 NB A:HEM801 2.1 14.1 1.0 NE2 A:HIS279 2.2 16.5 1.0 O2 A:TOX111 2.7 17.2 0.4 C4D A:HEM801 2.9 12.4 1.0 C1D A:HEM801 3.0 12.6 1.0 C1B A:HEM801 3.0 15.5 1.0 C1A A:HEM801 3.0 14.5 1.0 C1C A:HEM801 3.0 14.3 1.0 C4A A:HEM801 3.1 15.2 1.0 C4C A:HEM801 3.1 14.2 1.0 C4B A:HEM801 3.1 15.7 1.0 CD2 A:HIS279 3.1 14.3 1.0 CE1 A:HIS279 3.2 14.9 1.0 CHA A:HEM801 3.3 14.2 1.0 CHD A:HEM801 3.4 12.8 1.0 CHB A:HEM801 3.4 14.3 1.0 CHC A:HEM801 3.4 13.9 1.0 O1 A:TOX111 3.5 19.1 0.8 C3D A:HEM801 4.2 12.1 1.0 O1 A:OXY804 4.2 33.1 1.0 C2D A:HEM801 4.2 12.2 1.0 C2A A:HEM801 4.2 15.2 1.0 O2 A:TOX111 4.3 15.8 0.4 ND1 A:HIS279 4.3 15.2 1.0 C3A A:HEM801 4.3 14.8 1.0 C2B A:HEM801 4.3 15.7 1.0 C3C A:HEM801 4.3 15.4 1.0 NE1 A:TOX111 4.3 15.2 1.0 CG A:HIS279 4.3 15.6 1.0 C3B A:HEM801 4.3 15.3 1.0 C2C A:HEM801 4.3 15.0 1.0 CD1 A:TOX111 4.5 15.0 1.0 CH2 A:TRP330 5.0 15.6 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Burkholderia Pseudomallei Katg E242Q Variant


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 Burkholderia Pseudomallei Katg E242Q Variant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:16.2 occ:1.00 FE B:HEM801 0.0 16.2 1.0 NC B:HEM801 2.0 15.4 1.0 ND B:HEM801 2.0 15.6 1.0 NA B:HEM801 2.0 16.1 1.0 NB B:HEM801 2.1 16.1 1.0 NE2 B:HIS279 2.2 17.9 1.0 O2 B:TOX111 2.7 19.2 0.4 C1C B:HEM801 3.0 15.9 1.0 C1A B:HEM801 3.0 15.6 1.0 C4D B:HEM801 3.0 14.2 1.0 C4A B:HEM801 3.0 15.8 1.0 C4B B:HEM801 3.0 16.8 1.0 C1B B:HEM801 3.0 17.5 1.0 C1D B:HEM801 3.1 13.5 1.0 C4C B:HEM801 3.1 14.9 1.0 CE1 B:HIS279 3.2 16.0 1.0 CD2 B:HIS279 3.2 17.9 1.0 CHC B:HEM801 3.4 16.2 1.0 CHA B:HEM801 3.4 15.8 1.0 CHB B:HEM801 3.4 16.0 1.0 CHD B:HEM801 3.4 14.1 1.0 O1 B:TOX111 3.6 21.4 0.8 O2 B:TOX111 4.2 17.9 0.4 C2A B:HEM801 4.2 14.5 1.0 C3D B:HEM801 4.2 15.4 1.0 C2C B:HEM801 4.2 15.1 1.0 C2D B:HEM801 4.3 15.3 1.0 C3C B:HEM801 4.3 14.9 1.0 C3A B:HEM801 4.3 15.6 1.0 NE1 B:TOX111 4.3 15.8 1.0 ND1 B:HIS279 4.3 16.7 1.0 C2B B:HEM801 4.3 18.6 1.0 CG B:HIS279 4.3 17.9 1.0 C3B B:HEM801 4.3 17.2 1.0 O1 B:OXY804 4.4 28.3 1.0 CD1 B:TOX111 4.5 15.9 1.0 O B:HOH909 4.9 39.2 1.0

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