Iron in PDB 5fuk: Crystallization of A Dimeric Heme Peroxygenase From the Fungus Marasmius Rotula

All present enzymatic activity of Crystallization of A Dimeric Heme Peroxygenase From the Fungus Marasmius Rotula:
1.11.2.1;

The structure of Crystallization of A Dimeric Heme Peroxygenase From the Fungus Marasmius Rotula, PDB code: 5fuk was solved by K.Piontek, E.Strittmatter, D.A.Plattner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.36 / 1.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.010, 76.670, 120.800, 90.00, 90.00, 90.00
R / Rfree (%)	15.485 / 18.297

The structure of Crystallization of A Dimeric Heme Peroxygenase From the Fungus Marasmius Rotula also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Iron atom in the Crystallization of A Dimeric Heme Peroxygenase From the Fungus Marasmius Rotula (pdb code 5fuk). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystallization of A Dimeric Heme Peroxygenase From the Fungus Marasmius Rotula, PDB code: 5fuk:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystallization of A Dimeric Heme Peroxygenase From the Fungus Marasmius Rotula


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystallization of A Dimeric Heme Peroxygenase From the Fungus Marasmius Rotula within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1235 b:14.9 occ:1.00 FE A:HEM1235 0.0 14.9 1.0 ND A:HEM1235 2.0 13.4 1.0 NA A:HEM1235 2.0 14.1 1.0 NB A:HEM1235 2.0 14.0 1.0 NC A:HEM1235 2.0 14.6 1.0 O2 A:PLM1237 2.1 9.7 0.3 SG A:CYS17 2.4 15.5 1.0 C4D A:HEM1235 3.0 13.8 1.0 C1D A:HEM1235 3.0 13.2 1.0 C4B A:HEM1235 3.0 15.3 1.0 C1A A:HEM1235 3.0 13.5 1.0 C1B A:HEM1235 3.0 14.5 1.0 C1C A:HEM1235 3.0 14.4 1.0 C4C A:HEM1235 3.1 15.5 1.0 C4A A:HEM1235 3.1 13.2 1.0 C1 A:PLM1237 3.2 13.0 0.3 CHA A:HEM1235 3.4 14.8 1.0 CHC A:HEM1235 3.4 15.1 1.0 CHB A:HEM1235 3.4 14.7 1.0 CB A:CYS17 3.4 15.4 1.0 CHD A:HEM1235 3.4 13.8 1.0 O1 A:PLM1237 4.0 9.7 0.3 C2 A:PLM1237 4.2 18.1 0.3 C2A A:HEM1235 4.2 13.3 1.0 C2B A:HEM1235 4.2 15.7 1.0 C3C A:HEM1235 4.3 16.2 1.0 C3D A:HEM1235 4.3 13.2 1.0 C3A A:HEM1235 4.3 13.8 1.0 C2D A:HEM1235 4.3 13.1 1.0 C3B A:HEM1235 4.3 17.3 1.0 CA A:CYS17 4.3 14.4 1.0 C2C A:HEM1235 4.3 15.0 1.0 CD2 A:PHE160 4.6 18.4 0.4 CE2 A:PHE160 4.7 19.6 0.4 N A:GLY19 4.9 15.3 1.0 CG A:GLU157 4.9 15.7 1.0 OE2 A:GLU157 4.9 18.3 1.0 CD2 A:PHE160 5.0 23.8 0.6 C A:CYS17 5.0 14.7 1.0

Iron binding site 2 out of 2 in the Crystallization of A Dimeric Heme Peroxygenase From the Fungus Marasmius Rotula


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystallization of A Dimeric Heme Peroxygenase From the Fungus Marasmius Rotula within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1235 b:13.5 occ:1.00 FE B:HEM1235 0.0 13.5 1.0 ND B:HEM1235 1.9 13.0 1.0 NA B:HEM1235 2.0 13.0 1.0 NC B:HEM1235 2.0 13.6 1.0 NB B:HEM1235 2.1 13.3 1.0 O2 B:PLM1237 2.1 9.0 0.3 SG B:CYS17 2.3 14.2 1.0 C4D B:HEM1235 3.0 13.2 1.0 C1D B:HEM1235 3.0 13.3 1.0 C1A B:HEM1235 3.0 11.8 1.0 C4A B:HEM1235 3.0 12.8 1.0 C1C B:HEM1235 3.0 12.8 1.0 C4B B:HEM1235 3.0 13.5 1.0 C4C B:HEM1235 3.1 14.2 1.0 C1B B:HEM1235 3.1 13.1 1.0 C1 B:PLM1237 3.3 14.1 0.3 CHC B:HEM1235 3.4 13.4 1.0 CHB B:HEM1235 3.4 11.6 1.0 CHA B:HEM1235 3.4 13.1 1.0 CHD B:HEM1235 3.4 12.4 1.0 CB B:CYS17 3.5 13.0 1.0 O1 B:PLM1237 4.0 9.6 0.3 C2A B:HEM1235 4.2 14.0 1.0 C3D B:HEM1235 4.2 13.3 1.0 C3A B:HEM1235 4.2 11.8 1.0 C2D B:HEM1235 4.3 13.1 1.0 CA B:CYS17 4.3 13.1 1.0 C2B B:HEM1235 4.3 13.5 1.0 C3B B:HEM1235 4.3 14.1 1.0 C3C B:HEM1235 4.3 14.2 1.0 C2C B:HEM1235 4.3 13.8 1.0 C2 B:PLM1237 4.4 17.4 0.3 CD2 B:PHE160 4.7 19.5 0.4 CE2 B:PHE160 4.8 22.3 0.4 OE2 B:GLU157 4.9 17.8 1.0 CG B:GLU157 4.9 14.5 1.0 N B:GLY19 4.9 13.5 1.0 C B:CYS17 5.0 12.2 1.0

K.Piontek, E.Strittmatter, D.A.Plattner. Dimeric Heme Peroxygenase From Marasmius Rotula To Be Published.