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

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

The structure of Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei, PDB code: 5sxw 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 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.340, 116.020, 174.710, 90.00, 90.00, 90.00
R / Rfree (%)	14.3 / 16.9

The structure of Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Iron atom in the Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei (pdb code 5sxw). 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 Catalase-Peroxidase Katg of Burkholderia Pseudomallei, PDB code: 5sxw:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia 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 E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:13.4 occ:1.00 FE A:HEM801 0.0 13.4 1.0 ND A:HEM801 2.0 13.3 1.0 NC A:HEM801 2.0 14.3 1.0 NA A:HEM801 2.1 15.1 1.0 NB A:HEM801 2.1 13.6 1.0 NE2 A:HIS279 2.1 13.1 1.0 O2 A:TOX111 2.8 16.6 0.6 C1A A:HEM801 3.0 13.6 1.0 C1C A:HEM801 3.0 13.1 1.0 C1D A:HEM801 3.0 12.2 1.0 C4A A:HEM801 3.0 13.8 1.0 C4C A:HEM801 3.1 12.0 1.0 C1B A:HEM801 3.1 13.9 1.0 C4D A:HEM801 3.1 12.8 1.0 C4B A:HEM801 3.1 13.1 1.0 CE1 A:HIS279 3.1 14.3 1.0 CD2 A:HIS279 3.2 12.1 1.0 CHA A:HEM801 3.4 13.6 1.0 CHB A:HEM801 3.4 14.8 1.0 CHC A:HEM801 3.4 12.8 1.0 CHD A:HEM801 3.4 12.1 1.0 O1 A:TOX111 3.6 19.0 0.8 ND1 A:HIS279 4.2 14.6 1.0 C3A A:HEM801 4.2 13.7 1.0 NE1 A:TOX111 4.3 13.9 1.0 C3D A:HEM801 4.3 12.9 1.0 C2A A:HEM801 4.3 14.9 1.0 C2B A:HEM801 4.3 14.6 1.0 CG A:HIS279 4.3 13.3 1.0 C2D A:HEM801 4.3 11.8 1.0 C3C A:HEM801 4.3 11.9 1.0 C2C A:HEM801 4.3 12.6 1.0 C3B A:HEM801 4.3 14.7 1.0 O2 A:TOX111 4.3 12.4 0.2 O1 A:OXY803 4.5 28.1 1.0 CD1 A:TOX111 4.5 14.2 1.0 O A:HOH931 4.9 30.6 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia 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 E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:14.3 occ:1.00 FE B:HEM801 0.0 14.3 1.0 NA B:HEM801 2.0 14.4 1.0 NC B:HEM801 2.0 14.7 1.0 ND B:HEM801 2.0 14.2 1.0 NB B:HEM801 2.1 14.1 1.0 NE2 B:HIS279 2.2 15.3 1.0 O2 B:TOX111 2.7 17.4 0.7 C1A B:HEM801 3.0 13.6 1.0 C4C B:HEM801 3.0 12.6 1.0 C1C B:HEM801 3.0 13.2 1.0 C1B B:HEM801 3.0 13.6 1.0 C4B B:HEM801 3.0 14.1 1.0 C1D B:HEM801 3.0 13.0 1.0 C4D B:HEM801 3.1 14.7 1.0 C4A B:HEM801 3.1 14.4 1.0 CE1 B:HIS279 3.1 14.8 1.0 CD2 B:HIS279 3.2 15.1 1.0 CHA B:HEM801 3.4 13.4 1.0 CHB B:HEM801 3.4 13.4 1.0 CHD B:HEM801 3.4 12.5 1.0 CHC B:HEM801 3.4 14.1 1.0 O1 B:TOX111 3.6 21.6 1.0 O2 B:TOX111 4.2 12.8 0.3 C3D B:HEM801 4.2 13.1 1.0 C3A B:HEM801 4.2 14.2 1.0 ND1 B:HIS279 4.2 14.9 1.0 C2A B:HEM801 4.3 13.2 1.0 C2C B:HEM801 4.3 12.6 1.0 C2B B:HEM801 4.3 14.7 1.0 C3C B:HEM801 4.3 13.4 1.0 C2D B:HEM801 4.3 12.5 1.0 C3B B:HEM801 4.3 15.3 1.0 NE1 B:TOX111 4.3 14.2 1.0 CG B:HIS279 4.3 14.2 1.0 CD1 B:TOX111 4.5 13.5 1.0 O1 B:OXY803 4.5 24.8 1.0 O B:HOH1021 5.0 33.0 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