Iron in PDB 6b9b: Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose Bound

All present enzymatic activity of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose Bound:
1.11.1.21;

The structure of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose Bound, PDB code: 6b9b 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)	50.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.419, 115.088, 174.975, 90.00, 90.00, 90.00
R / Rfree (%)	13.5 / 16.2

The structure of Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose Bound 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 Catalase-Peroxidase From B. Pseudomallei with Maltose Bound (pdb code 6b9b). 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 From B. Pseudomallei with Maltose Bound, PDB code: 6b9b:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose Bound


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 From B. Pseudomallei with Maltose Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:19.1 occ:1.00 FE A:HEM801 0.0 19.1 1.0 ND A:HEM801 2.0 18.5 1.0 NA A:HEM801 2.0 20.4 1.0 NC A:HEM801 2.1 17.2 1.0 NB A:HEM801 2.1 17.3 1.0 NE2 A:HIS279 2.2 21.5 1.0 O2 A:TOX111 2.7 20.2 0.6 C4D A:HEM801 3.0 17.9 1.0 C1D A:HEM801 3.0 16.7 1.0 C4A A:HEM801 3.0 19.7 1.0 C1C A:HEM801 3.1 16.7 1.0 C4C A:HEM801 3.1 15.7 1.0 C1B A:HEM801 3.1 19.6 1.0 C4B A:HEM801 3.1 18.1 1.0 C1A A:HEM801 3.1 17.0 1.0 CD2 A:HIS279 3.2 18.6 1.0 CE1 A:HIS279 3.2 21.4 1.0 CHD A:HEM801 3.4 17.5 1.0 CHB A:HEM801 3.4 19.9 1.0 CHC A:HEM801 3.4 18.2 1.0 CHA A:HEM801 3.4 18.8 1.0 O1 A:TOX111 3.6 22.4 0.7 C3D A:HEM801 4.2 18.1 1.0 NE1 A:TOX111 4.2 19.0 1.0 C2D A:HEM801 4.2 17.6 1.0 C2A A:HEM801 4.3 18.8 1.0 C3A A:HEM801 4.3 19.1 1.0 C2B A:HEM801 4.3 19.7 1.0 C3C A:HEM801 4.3 17.1 1.0 C2C A:HEM801 4.3 16.2 1.0 ND1 A:HIS279 4.3 20.5 1.0 C3B A:HEM801 4.3 18.7 1.0 CG A:HIS279 4.4 19.3 1.0 O2 A:TOX111 4.4 17.6 0.1 O1 A:OXY804 4.4 35.4 1.0 CD1 A:TOX111 4.5 19.4 1.0 O A:HOH949 4.7 40.0 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Catalase-Peroxidase From B. Pseudomallei with Maltose Bound


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 From B. Pseudomallei with Maltose Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:18.7 occ:1.00 FE B:HEM801 0.0 18.7 1.0 NA B:HEM801 2.0 17.4 1.0 ND B:HEM801 2.0 16.2 1.0 NC B:HEM801 2.0 17.5 1.0 NB B:HEM801 2.0 16.8 1.0 NE2 B:HIS279 2.2 19.5 1.0 O2 B:TOX111 2.8 22.5 0.8 C4C B:HEM801 3.0 16.7 1.0 C4B B:HEM801 3.0 17.0 1.0 C1C B:HEM801 3.0 15.4 1.0 C1A B:HEM801 3.0 15.9 1.0 C4A B:HEM801 3.0 17.7 1.0 C4D B:HEM801 3.0 15.0 1.0 C1B B:HEM801 3.0 18.9 1.0 C1D B:HEM801 3.1 16.2 1.0 CD2 B:HIS279 3.2 19.2 1.0 CE1 B:HIS279 3.2 19.1 1.0 CHA B:HEM801 3.4 15.3 1.0 CHC B:HEM801 3.4 17.1 1.0 CHD B:HEM801 3.4 15.7 1.0 CHB B:HEM801 3.4 18.1 1.0 O1 B:TOX111 3.6 23.4 0.9 NE1 B:TOX111 4.2 17.8 1.0 C3A B:HEM801 4.2 18.4 1.0 C3D B:HEM801 4.2 16.7 1.0 C2D B:HEM801 4.2 16.2 1.0 C3C B:HEM801 4.3 16.3 1.0 C2A B:HEM801 4.3 17.2 1.0 C2C B:HEM801 4.3 16.2 1.0 O2 B:TOX111 4.3 18.5 0.1 C2B B:HEM801 4.3 17.6 1.0 C3B B:HEM801 4.3 17.9 1.0 ND1 B:HIS279 4.3 17.6 1.0 CG B:HIS279 4.3 18.5 1.0 CD1 B:TOX111 4.5 19.5 1.0 O1 B:OXY804 4.7 30.9 1.0 O B:HOH941 4.7 36.9 1.0

P.C.Loewen, P.M.De Silva, L.J.Donald, J.Switala, J.Villanueva, I.Fita, A.Kumar. Katg-Mediated Oxidation Leading to Reduced Susceptibility of Bacteria to Kanamycin. Acs Omega V. 3 4213 2018.
ISSN: ESSN 2470-1343
PubMed: 29732452
DOI: 10.1021/ACSOMEGA.8B00356