Iron in PDB 5cif: Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C

All present enzymatic activity of Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C:
1.11.1.5;

The structure of Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C, PDB code: 5cif was solved by B.R.Crane, T.M.Payne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.43 / 2.01
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.797, 113.842, 88.239, 90.00, 105.31, 90.00
R / Rfree (%)	21.6 / 26.8

The binding sites of Iron atom in the Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C (pdb code 5cif). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C, PDB code: 5cif:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:21.0 occ:1.00 FE A:HEM301 0.0 21.0 1.0 NC A:HEM301 2.0 13.8 1.0 NE2 A:HIS175 2.0 24.7 1.0 NB A:HEM301 2.0 27.5 1.0 NA A:HEM301 2.1 21.1 1.0 ND A:HEM301 2.1 15.9 1.0 CE1 A:HIS175 3.0 25.6 1.0 C1B A:HEM301 3.0 23.1 1.0 C4B A:HEM301 3.0 26.0 1.0 C4C A:HEM301 3.0 24.2 1.0 C1C A:HEM301 3.0 22.9 1.0 CD2 A:HIS175 3.1 25.3 1.0 C4A A:HEM301 3.1 23.5 1.0 C1D A:HEM301 3.1 22.2 1.0 C1A A:HEM301 3.1 29.7 1.0 C4D A:HEM301 3.1 20.0 1.0 CHC A:HEM301 3.4 21.8 1.0 CHB A:HEM301 3.4 24.1 1.0 CHD A:HEM301 3.4 16.1 1.0 CHA A:HEM301 3.5 23.3 1.0 ND1 A:HIS175 4.1 26.1 1.0 CG A:HIS175 4.2 29.3 1.0 C2B A:HEM301 4.2 20.9 1.0 C3B A:HEM301 4.2 22.4 1.0 C2C A:HEM301 4.3 15.7 1.0 C3C A:HEM301 4.3 19.3 1.0 C3A A:HEM301 4.3 28.8 1.0 C2D A:HEM301 4.3 21.0 1.0 NE1 A:TRP51 4.3 13.4 1.0 C2A A:HEM301 4.3 30.6 1.0 C3D A:HEM301 4.3 16.4 1.0 CD1 A:TRP51 4.7 12.6 1.0 O A:HOH545 4.8 43.9 1.0

Iron binding site 2 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:25.5 occ:1.00 FE B:HEM201 0.0 25.5 1.0 NE2 B:HIS18 2.0 27.1 1.0 NC B:HEM201 2.0 18.7 1.0 NB B:HEM201 2.0 22.6 1.0 ND B:HEM201 2.0 37.4 1.0 NA B:HEM201 2.1 22.0 1.0 SD B:MET80 2.3 23.7 1.0 CE1 B:HIS18 2.9 22.7 1.0 C4C B:HEM201 3.0 22.7 1.0 C1D B:HEM201 3.0 31.5 1.0 C1C B:HEM201 3.0 26.3 1.0 C4B B:HEM201 3.0 30.5 1.0 CD2 B:HIS18 3.1 33.3 1.0 C1B B:HEM201 3.1 26.6 1.0 C4D B:HEM201 3.1 39.4 1.0 C1A B:HEM201 3.1 22.4 1.0 C4A B:HEM201 3.1 25.3 1.0 CG B:MET80 3.3 20.2 1.0 CHD B:HEM201 3.4 24.5 1.0 CHC B:HEM201 3.4 31.1 1.0 CHA B:HEM201 3.4 24.0 1.0 CHB B:HEM201 3.4 23.8 1.0 CE B:MET80 3.4 17.6 1.0 ND1 B:HIS18 4.0 21.8 1.0 CG B:HIS18 4.1 28.0 1.0 CB B:MET80 4.1 19.1 1.0 C3C B:HEM201 4.2 17.4 1.0 C2C B:HEM201 4.3 21.8 1.0 C3B B:HEM201 4.3 27.2 1.0 C2D B:HEM201 4.3 32.8 1.0 C2B B:HEM201 4.3 24.5 1.0 C3D B:HEM201 4.3 34.6 1.0 C2A B:HEM201 4.3 25.5 1.0 C3A B:HEM201 4.3 38.7 1.0 OH B:TYR67 4.8 25.9 1.0

Iron binding site 3 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:17.3 occ:1.00 FE C:HEM301 0.0 17.3 1.0 NE2 C:HIS175 2.0 22.8 1.0 NC C:HEM301 2.1 11.5 1.0 NA C:HEM301 2.1 14.3 1.0 ND C:HEM301 2.1 11.2 1.0 NB C:HEM301 2.1 19.5 1.0 O C:HOH514 2.8 39.1 1.0 CE1 C:HIS175 3.0 22.4 1.0 CD2 C:HIS175 3.1 22.4 1.0 C1D C:HEM301 3.1 14.2 1.0 C4C C:HEM301 3.1 16.8 1.0 C1B C:HEM301 3.1 18.5 1.0 C4A C:HEM301 3.1 18.9 1.0 C4D C:HEM301 3.1 16.2 1.0 C1A C:HEM301 3.1 15.2 1.0 C1C C:HEM301 3.1 13.2 1.0 C4B C:HEM301 3.1 18.8 1.0 CHD C:HEM301 3.4 17.1 1.0 CHA C:HEM301 3.4 13.9 1.0 CHB C:HEM301 3.5 18.7 1.0 CHC C:HEM301 3.5 18.7 1.0 ND1 C:HIS175 4.1 20.1 1.0 CG C:HIS175 4.2 25.0 1.0 C2B C:HEM301 4.3 14.0 1.0 C2D C:HEM301 4.3 12.1 1.0 C3A C:HEM301 4.3 15.1 1.0 C3B C:HEM301 4.3 20.0 1.0 C3C C:HEM301 4.3 18.0 1.0 C3D C:HEM301 4.3 15.6 1.0 C2A C:HEM301 4.3 17.4 1.0 C2C C:HEM301 4.3 14.6 1.0 NE1 C:TRP51 4.4 15.9 1.0 CD1 C:TRP51 4.7 15.2 1.0 O C:HOH531 5.0 42.7 1.0

Iron binding site 4 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Complex of Yeast Cytochrome C Peroxidase (W191F) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:30.7 occ:1.00 FE D:HEM201 0.0 30.7 1.0 NE2 D:HIS18 2.0 39.8 1.0 ND D:HEM201 2.0 30.7 1.0 NB D:HEM201 2.0 23.0 1.0 NA D:HEM201 2.0 38.2 1.0 NC D:HEM201 2.1 19.6 1.0 SD D:MET80 2.3 29.5 1.0 CD2 D:HIS18 2.9 48.3 1.0 C1D D:HEM201 3.0 39.0 1.0 C4D D:HEM201 3.0 37.8 1.0 C1B D:HEM201 3.0 29.6 1.0 CE1 D:HIS18 3.0 48.4 1.0 C4A D:HEM201 3.0 29.6 1.0 C4B D:HEM201 3.0 31.3 1.0 C1A D:HEM201 3.1 38.0 1.0 C4C D:HEM201 3.1 27.5 1.0 C1C D:HEM201 3.1 24.4 1.0 CE D:MET80 3.2 27.4 1.0 CHA D:HEM201 3.4 34.3 1.0 CHD D:HEM201 3.4 38.3 1.0 CHB D:HEM201 3.4 28.4 1.0 CHC D:HEM201 3.4 23.6 1.0 CG D:MET80 3.4 41.4 1.0 CG D:HIS18 4.1 46.1 1.0 ND1 D:HIS18 4.1 46.5 1.0 C2B D:HEM201 4.2 35.0 1.0 C3B D:HEM201 4.3 27.9 1.0 C2D D:HEM201 4.3 41.4 1.0 C3D D:HEM201 4.3 40.4 1.0 C3A D:HEM201 4.3 34.0 1.0 C2A D:HEM201 4.3 40.3 1.0 C3C D:HEM201 4.3 38.3 1.0 C2C D:HEM201 4.3 33.7 1.0 CB D:MET80 4.3 34.0 1.0

T.M.Payne, E.F.Yee, B.Dzikovski, B.R.Crane. Constraints on the Radical Cation Center of Cytochrome C Peroxidase For Electron Transfer From Cytochrome C. Biochemistry V. 55 4807 2016.
ISSN: ISSN 0006-2960
PubMed: 27499202
DOI: 10.1021/ACS.BIOCHEM.6B00262