Iron in PDB 3hq6: Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type

All present enzymatic activity of Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type:
1.11.1.5;

The structure of Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type, PDB code: 3hq6 was solved by M.Hoffmann, J.Seidel, O.Einsle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.00 / 2.00
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	54.241, 55.783, 78.644, 68.69, 71.84, 57.76
R / Rfree (%)	18.9 / 26.6

The structure of Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Iron atom in the Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type (pdb code 3hq6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type, PDB code: 3hq6:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:14.5 occ:1.00 FE A:HEM400 0.0 14.5 1.0 NB A:HEM400 2.0 17.6 1.0 NA A:HEM400 2.0 17.0 1.0 ND A:HEM400 2.0 16.2 1.0 NE2 A:HIS93 2.0 9.3 1.0 NC A:HEM400 2.1 16.1 1.0 NE2 A:HIS77 2.1 14.4 1.0 C4A A:HEM400 2.9 13.5 1.0 CD2 A:HIS93 2.9 11.2 1.0 CE1 A:HIS77 2.9 13.3 1.0 C1D A:HEM400 3.0 12.6 1.0 C1B A:HEM400 3.0 18.3 1.0 C4C A:HEM400 3.0 15.6 1.0 C4D A:HEM400 3.1 14.1 1.0 C4B A:HEM400 3.1 12.8 1.0 CE1 A:HIS93 3.1 11.7 1.0 C1C A:HEM400 3.1 11.5 1.0 C1A A:HEM400 3.1 14.3 1.0 CD2 A:HIS77 3.1 15.8 1.0 CHB A:HEM400 3.3 16.1 1.0 CHD A:HEM400 3.4 12.6 1.0 CHC A:HEM400 3.5 15.9 1.0 CHA A:HEM400 3.5 12.1 1.0 ND1 A:HIS77 4.1 18.5 1.0 CG A:HIS93 4.1 13.2 1.0 ND1 A:HIS93 4.1 11.4 1.0 C3A A:HEM400 4.2 11.9 1.0 C2D A:HEM400 4.2 13.0 1.0 CG A:HIS77 4.2 15.7 1.0 C3D A:HEM400 4.2 15.1 1.0 C3B A:HEM400 4.2 13.8 1.0 C2B A:HEM400 4.2 14.8 1.0 C2A A:HEM400 4.3 14.4 1.0 C3C A:HEM400 4.3 14.2 1.0 C2C A:HEM400 4.3 16.3 1.0

Iron binding site 2 out of 4 in the Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:19.1 occ:1.00 FE A:HEM401 0.0 19.1 1.0 NE2 A:HIS223 2.0 9.8 1.0 ND A:HEM401 2.0 18.8 1.0 NA A:HEM401 2.0 19.8 1.0 NC A:HEM401 2.1 23.1 1.0 SD A:MET297 2.1 19.2 1.0 NB A:HEM401 2.1 22.6 1.0 CE1 A:HIS223 3.0 12.0 1.0 C1D A:HEM401 3.0 18.6 1.0 C4C A:HEM401 3.0 22.8 1.0 C4D A:HEM401 3.0 21.6 1.0 C1A A:HEM401 3.1 20.6 1.0 C4A A:HEM401 3.1 20.6 1.0 CD2 A:HIS223 3.1 19.4 1.0 C1B A:HEM401 3.1 23.8 1.0 C1C A:HEM401 3.1 21.6 1.0 C4B A:HEM401 3.2 23.1 1.0 CG A:MET297 3.3 21.5 1.0 CHD A:HEM401 3.3 21.8 1.0 CHA A:HEM401 3.4 20.4 1.0 CHB A:HEM401 3.4 21.7 1.0 CE A:MET297 3.5 19.8 1.0 CHC A:HEM401 3.5 23.0 1.0 ND1 A:HIS223 4.1 14.6 1.0 CG A:HIS223 4.2 14.1 1.0 C2D A:HEM401 4.2 15.9 1.0 C3D A:HEM401 4.2 16.7 1.0 C3C A:HEM401 4.2 21.3 1.0 C3A A:HEM401 4.3 19.6 1.0 C2A A:HEM401 4.3 19.9 1.0 CB A:MET297 4.3 19.7 1.0 C2C A:HEM401 4.3 21.6 1.0 C2B A:HEM401 4.3 24.5 1.0 C3B A:HEM401 4.4 23.3 1.0

Iron binding site 3 out of 4 in the Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe400 b:15.7 occ:1.00 FE B:HEM400 0.0 15.7 1.0 NE2 B:HIS93 2.0 15.4 1.0 ND B:HEM400 2.0 14.5 1.0 NA B:HEM400 2.0 11.5 1.0 NC B:HEM400 2.0 12.5 1.0 NE2 B:HIS77 2.0 15.2 1.0 NB B:HEM400 2.1 15.8 1.0 CD2 B:HIS93 2.9 11.2 1.0 CE1 B:HIS77 3.0 15.1 1.0 CE1 B:HIS93 3.0 14.5 1.0 C4A B:HEM400 3.0 11.0 1.0 C4C B:HEM400 3.0 12.7 1.0 C4D B:HEM400 3.0 15.7 1.0 C1B B:HEM400 3.0 10.6 1.0 C1D B:HEM400 3.0 13.9 1.0 C1A B:HEM400 3.1 13.0 1.0 CD2 B:HIS77 3.1 8.9 1.0 C4B B:HEM400 3.1 14.7 1.0 C1C B:HEM400 3.1 8.1 1.0 CHB B:HEM400 3.4 11.8 1.0 CHD B:HEM400 3.4 8.6 1.0 CHA B:HEM400 3.4 10.4 1.0 CHC B:HEM400 3.5 13.3 1.0 ND1 B:HIS93 4.1 12.5 1.0 CG B:HIS93 4.1 15.0 1.0 ND1 B:HIS77 4.1 15.4 1.0 CG B:HIS77 4.2 15.0 1.0 C3D B:HEM400 4.2 12.9 1.0 C3A B:HEM400 4.2 9.1 1.0 C2D B:HEM400 4.2 9.2 1.0 C2B B:HEM400 4.2 16.3 1.0 C2A B:HEM400 4.2 12.7 1.0 C3C B:HEM400 4.3 12.1 1.0 C3B B:HEM400 4.3 11.6 1.0 C2C B:HEM400 4.3 14.7 1.0

Iron binding site 4 out of 4 in the Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cytochrome C Peroxidase From G. Sulfurreducens, Wild Type within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:16.9 occ:1.00 FE B:HEM401 0.0 16.9 1.0 NA B:HEM401 2.0 20.5 1.0 NC B:HEM401 2.0 17.9 1.0 NB B:HEM401 2.0 19.3 1.0 NE2 B:HIS223 2.0 14.6 1.0 ND B:HEM401 2.1 16.3 1.0 SD B:MET297 2.3 19.2 1.0 CE1 B:HIS223 3.0 12.7 1.0 C4A B:HEM401 3.0 18.6 1.0 C4C B:HEM401 3.0 18.8 1.0 C1D B:HEM401 3.1 15.4 1.0 C1B B:HEM401 3.1 21.6 1.0 C4B B:HEM401 3.1 21.4 1.0 C1C B:HEM401 3.1 18.2 1.0 C1A B:HEM401 3.1 15.9 1.0 CD2 B:HIS223 3.1 9.8 1.0 C4D B:HEM401 3.2 19.0 1.0 CHD B:HEM401 3.3 17.2 1.0 CG B:MET297 3.4 18.1 1.0 CHB B:HEM401 3.4 19.5 1.0 CHC B:HEM401 3.4 18.2 1.0 CHA B:HEM401 3.5 17.9 1.0 CE B:MET297 3.7 12.1 1.0 ND1 B:HIS223 4.1 14.0 1.0 CG B:HIS223 4.2 14.6 1.0 C3A B:HEM401 4.2 15.2 1.0 C3C B:HEM401 4.2 18.5 1.0 C2C B:HEM401 4.3 16.3 1.0 C2A B:HEM401 4.3 13.8 1.0 C3B B:HEM401 4.3 20.7 1.0 C2B B:HEM401 4.3 21.9 1.0 C2D B:HEM401 4.3 17.2 1.0 CB B:MET297 4.4 18.0 1.0 C3D B:HEM401 4.4 17.4 1.0

M.Hoffmann, J.Seidel, O.Einsle. Ccpa From Geobacter Sulfurreducens Is A Basic Di-Heme Cytochrome C Peroxidase. J.Mol.Biol. V. 393 951 2009.
ISSN: ISSN 0022-2836
PubMed: 19735665
DOI: 10.1016/J.JMB.2009.09.001