Iron in PDB 5kq0: Crystal Structure of the A290D Variant of Catalase-Peroxidase From B. Pseudomallei

All present enzymatic activity of Crystal Structure of the A290D Variant of Catalase-Peroxidase From B. Pseudomallei:
1.11.1.21;

The structure of Crystal Structure of the A290D Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kq0 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)	95.14 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.760, 113.490, 174.513, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 18.5

The structure of Crystal Structure of the A290D Variant of Catalase-Peroxidase From B. Pseudomallei 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 the A290D Variant of Catalase-Peroxidase From B. Pseudomallei (pdb code 5kq0). 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 A290D Variant of Catalase-Peroxidase From B. Pseudomallei, PDB code: 5kq0:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the A290D Variant of Catalase-Peroxidase From B. Pseudomallei


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 A290D Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:17.7 occ:1.00 FE A:HEM801 0.0 17.7 1.0 NC A:HEM801 2.0 17.5 1.0 ND A:HEM801 2.0 14.7 1.0 NA A:HEM801 2.0 17.9 1.0 NE2 A:HIS279 2.1 19.8 1.0 NB A:HEM801 2.1 16.9 1.0 O2 A:TOX111 2.8 32.5 0.9 C1D A:HEM801 3.0 15.2 1.0 C4D A:HEM801 3.0 16.2 1.0 C1B A:HEM801 3.0 17.3 1.0 C1C A:HEM801 3.0 18.1 1.0 C1A A:HEM801 3.0 16.5 1.0 C4C A:HEM801 3.0 17.3 1.0 C4B A:HEM801 3.1 18.5 1.0 C4A A:HEM801 3.1 17.6 1.0 CD2 A:HIS279 3.1 18.7 1.0 CE1 A:HIS279 3.1 19.5 1.0 CHA A:HEM801 3.4 15.8 1.0 CHD A:HEM801 3.4 15.4 1.0 CHC A:HEM801 3.4 17.2 1.0 CHB A:HEM801 3.4 16.6 1.0 O1 A:TOX111 3.6 27.1 0.9 C2D A:HEM801 4.2 15.1 1.0 C3C A:HEM801 4.2 16.8 1.0 C3D A:HEM801 4.3 15.3 1.0 ND1 A:HIS279 4.3 18.5 1.0 C2C A:HEM801 4.3 16.5 1.0 CG A:HIS279 4.3 19.3 1.0 C3A A:HEM801 4.3 17.8 1.0 NE1 A:TOX111 4.3 19.6 1.0 C2B A:HEM801 4.3 19.1 1.0 C2A A:HEM801 4.3 19.3 1.0 C3B A:HEM801 4.3 18.3 1.0 O1 A:OXY804 4.5 38.7 1.0 CD1 A:TOX111 4.5 18.5 1.0 O A:HOH1197 4.8 35.1 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the A290D Variant of Catalase-Peroxidase From B. Pseudomallei


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 A290D Variant of Catalase-Peroxidase From B. Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:17.8 occ:1.00 FE B:HEM801 0.0 17.8 1.0 ND B:HEM801 1.9 16.4 1.0 NC B:HEM801 2.0 17.1 1.0 NB B:HEM801 2.0 18.3 1.0 NA B:HEM801 2.1 16.3 1.0 NE2 B:HIS279 2.1 19.2 1.0 O2 B:TOX111 2.8 27.5 1.0 C1C B:HEM801 3.0 17.4 1.0 C4D B:HEM801 3.0 15.3 1.0 C4B B:HEM801 3.0 18.0 1.0 C4C B:HEM801 3.0 15.5 1.0 C1D B:HEM801 3.0 14.6 1.0 C4A B:HEM801 3.0 16.6 1.0 C1A B:HEM801 3.1 16.6 1.0 C1B B:HEM801 3.1 18.1 1.0 CD2 B:HIS279 3.1 17.8 1.0 CE1 B:HIS279 3.1 18.6 1.0 CHC B:HEM801 3.3 18.3 1.0 CHA B:HEM801 3.4 16.0 1.0 CHB B:HEM801 3.4 17.0 1.0 CHD B:HEM801 3.5 15.7 1.0 O1 B:TOX111 3.6 25.9 1.0 C3D B:HEM801 4.2 16.1 1.0 C2D B:HEM801 4.2 15.3 1.0 C2C B:HEM801 4.2 16.6 1.0 C3A B:HEM801 4.3 15.7 1.0 C2A B:HEM801 4.3 15.3 1.0 ND1 B:HIS279 4.3 18.6 1.0 C3B B:HEM801 4.3 17.6 1.0 C3C B:HEM801 4.3 16.2 1.0 CG B:HIS279 4.3 18.8 1.0 NE1 B:TOX111 4.3 19.6 1.0 C2B B:HEM801 4.3 18.2 1.0 CD1 B:TOX111 4.5 20.4 1.0 O B:HOH1257 4.8 34.6 1.0 O1 B:OXY804 4.8 38.2 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