Iron in PDB 5sx0: Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5

All present enzymatic activity of Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5:
1.11.1.21;

The structure of Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5, PDB code: 5sx0 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 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.359, 114.886, 174.626, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 19.4

The structure of Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5 also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Iron atom in the Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5 (pdb code 5sx0). 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 An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5, PDB code: 5sx0:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5


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 An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:22.5 occ:1.00 FE A:HEM801 0.0 22.5 1.0 ND A:HEM801 1.9 21.8 1.0 NE2 A:HIS279 2.0 22.4 1.0 O A:O805 2.0 27.2 1.0 NA A:HEM801 2.0 22.6 1.0 NB A:HEM801 2.1 22.8 1.0 NC A:HEM801 2.1 21.4 1.0 CE1 A:HIS279 3.0 22.7 1.0 C4D A:HEM801 3.0 22.3 1.0 C1D A:HEM801 3.0 21.8 1.0 C1B A:HEM801 3.0 24.4 1.0 CD2 A:HIS279 3.0 22.2 1.0 C4C A:HEM801 3.0 21.4 1.0 C4A A:HEM801 3.1 24.3 1.0 C1A A:HEM801 3.1 23.6 1.0 C1C A:HEM801 3.1 21.7 1.0 C4B A:HEM801 3.1 23.6 1.0 CHB A:HEM801 3.4 24.9 1.0 CHD A:HEM801 3.4 21.7 1.0 CHA A:HEM801 3.4 23.2 1.0 CHC A:HEM801 3.5 22.1 1.0 O1 A:OXY804 4.0 48.7 1.0 O1 A:OXY803 4.0 35.9 1.0 ND1 A:HIS279 4.1 23.4 1.0 CG A:HIS279 4.2 22.4 1.0 NE1 A:TRP111 4.2 22.2 1.0 C2D A:HEM801 4.2 23.0 1.0 C3D A:HEM801 4.2 22.7 1.0 C2B A:HEM801 4.3 24.4 1.0 C3A A:HEM801 4.3 25.6 1.0 C2A A:HEM801 4.3 25.0 1.0 C3C A:HEM801 4.3 21.4 1.0 C2C A:HEM801 4.3 21.0 1.0 C3B A:HEM801 4.3 23.9 1.0 CD1 A:TRP111 4.4 21.4 1.0 O2 A:OXY804 4.5 51.5 1.0

Iron binding site 2 out of 2 in the Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5


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 An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:21.1 occ:1.00 FE B:HEM801 0.0 21.1 1.0 ND B:HEM801 1.9 20.2 1.0 NE2 B:HIS279 2.0 21.4 1.0 O B:O804 2.0 22.0 1.0 NA B:HEM801 2.0 20.0 1.0 NB B:HEM801 2.0 20.6 1.0 NC B:HEM801 2.1 20.7 1.0 C4D B:HEM801 3.0 19.4 1.0 C1D B:HEM801 3.0 21.2 1.0 CE1 B:HIS279 3.0 23.0 1.0 C4B B:HEM801 3.0 21.1 1.0 C1A B:HEM801 3.0 19.9 1.0 CD2 B:HIS279 3.0 24.0 1.0 C1B B:HEM801 3.0 21.9 1.0 C4C B:HEM801 3.0 20.7 1.0 C4A B:HEM801 3.1 22.5 1.0 C1C B:HEM801 3.1 19.7 1.0 CHC B:HEM801 3.4 20.9 1.0 CHA B:HEM801 3.4 20.1 1.0 CHD B:HEM801 3.4 20.5 1.0 CHB B:HEM801 3.4 21.6 1.0 O B:HOH1941 4.0 35.0 1.0 NE1 B:TRP111 4.1 21.8 1.0 ND1 B:HIS279 4.1 22.8 1.0 O1 B:OXY803 4.2 39.5 1.0 CG B:HIS279 4.2 22.1 1.0 C2D B:HEM801 4.2 21.5 1.0 C3D B:HEM801 4.2 20.5 1.0 C2A B:HEM801 4.2 20.7 1.0 C2C B:HEM801 4.2 20.3 1.0 C3A B:HEM801 4.3 22.4 1.0 C3C B:HEM801 4.3 20.9 1.0 C2B B:HEM801 4.3 20.3 1.0 C3B B:HEM801 4.3 21.4 1.0 CD1 B:TRP111 4.4 21.6 1.0

X.Carpena, B.Wiseman, T.Deemagarn, R.Singh, J.Switala, A.Ivancich, I.Fita, P.C.Loewen. A Molecular Switch and Electronic Circuit Modulate Catalase Activity in Catalase-Peroxidases. Embo Rep. V. 6 1156 2005.
ISSN: ISSN 1469-221X
PubMed: 16211084