Iron in PDB 5sxx: Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh

All present enzymatic activity of Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh:
1.11.1.21;

The structure of Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh, PDB code: 5sxx 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 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.570, 115.940, 174.730, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / 16.9

The structure of Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh 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 E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh (pdb code 5sxx). 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 E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh, PDB code: 5sxx:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh


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 E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:13.6 occ:1.00 FE A:HEM801 0.0 13.6 1.0 ND A:HEM801 2.0 13.5 1.0 NA A:HEM801 2.0 15.5 1.0 NE2 A:HIS279 2.1 16.1 1.0 NB A:HEM801 2.1 14.2 1.0 NC A:HEM801 2.1 13.4 1.0 O A:HOH963 2.6 34.3 1.0 C4D A:HEM801 3.0 13.2 1.0 C1A A:HEM801 3.0 13.7 1.0 C1C A:HEM801 3.0 12.7 1.0 C4B A:HEM801 3.0 14.5 1.0 C4C A:HEM801 3.1 11.4 1.0 C1B A:HEM801 3.1 15.1 1.0 CD2 A:HIS279 3.1 14.7 1.0 C4A A:HEM801 3.1 14.8 1.0 C1D A:HEM801 3.1 12.2 1.0 CE1 A:HIS279 3.1 15.1 1.0 CHA A:HEM801 3.4 14.0 1.0 CHB A:HEM801 3.4 15.5 1.0 CHC A:HEM801 3.5 12.8 1.0 CHD A:HEM801 3.5 11.8 1.0 ND1 A:HIS279 4.2 15.4 1.0 C2B A:HEM801 4.2 16.1 1.0 CG A:HIS279 4.2 14.1 1.0 C3D A:HEM801 4.3 12.6 1.0 C3A A:HEM801 4.3 14.2 1.0 C2C A:HEM801 4.3 11.5 1.0 C3B A:HEM801 4.3 14.1 1.0 C2A A:HEM801 4.3 15.2 1.0 C3C A:HEM801 4.3 12.9 1.0 C2D A:HEM801 4.3 11.2 1.0 NE1 A:TRP111 4.4 14.2 1.0 O1 A:OXY804 4.4 32.2 1.0 O1 A:OXY805 4.4 34.7 1.0 O2 A:OXY805 4.5 60.1 1.0 CD1 A:TRP111 4.7 13.7 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh


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 E198A Variant of Burkholderia Pseudomallei Catalase-Peroxidase Katg with Inh within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:13.2 occ:1.00 FE B:HEM801 0.0 13.2 1.0 NA B:HEM801 2.0 14.2 1.0 NB B:HEM801 2.0 12.6 1.0 ND B:HEM801 2.0 12.6 1.0 NC B:HEM801 2.0 12.4 1.0 NE2 B:HIS279 2.1 13.9 1.0 O B:HOH905 2.5 28.5 1.0 C1A B:HEM801 3.0 12.7 1.0 C1C B:HEM801 3.0 11.7 1.0 C4B B:HEM801 3.0 12.6 1.0 C4D B:HEM801 3.0 12.5 1.0 C1D B:HEM801 3.0 11.8 1.0 C1B B:HEM801 3.0 14.7 1.0 C4C B:HEM801 3.1 11.2 1.0 C4A B:HEM801 3.1 14.2 1.0 CD2 B:HIS279 3.1 13.6 1.0 CE1 B:HIS279 3.1 14.4 1.0 CHB B:HEM801 3.4 14.1 1.0 CHD B:HEM801 3.4 10.9 1.0 CHA B:HEM801 3.4 12.2 1.0 CHC B:HEM801 3.5 12.3 1.0 O2 B:OXY805 3.9 42.5 1.0 ND1 B:HIS279 4.2 14.6 1.0 C2C B:HEM801 4.2 11.9 1.0 CG B:HIS279 4.2 13.6 1.0 C3A B:HEM801 4.3 14.5 1.0 C2A B:HEM801 4.3 13.4 1.0 C3C B:HEM801 4.3 11.8 1.0 C3D B:HEM801 4.3 12.5 1.0 C2B B:HEM801 4.3 14.1 1.0 C2D B:HEM801 4.3 11.3 1.0 C3B B:HEM801 4.3 13.6 1.0 NE1 B:TRP111 4.4 12.3 1.0 O1 B:OXY805 4.4 34.0 1.0 O1 B:OXY804 4.6 26.4 1.0 CD1 B:TRP111 4.7 12.2 1.0

B.Wiseman, X.Carpena, M.Feliz, L.J.Donald, M.Pons, I.Fita, P.C.Loewen. Isonicotinic Acid Hydrazide Conversion to Isonicotinyl-Nad By Catalase-Peroxidases. J. Biol. Chem. V. 285 26662 2010.
ISSN: ESSN 1083-351X
PubMed: 20554537
DOI: 10.1074/JBC.M110.139428