Iron in PDB 5cih: Complex of Yeast Cytochrome C Peroxidase (W191Y) with Iso-1 Cytochrome C

All present enzymatic activity of Complex of Yeast Cytochrome C Peroxidase (W191Y) with Iso-1 Cytochrome C:
1.11.1.5;

The structure of Complex of Yeast Cytochrome C Peroxidase (W191Y) with Iso-1 Cytochrome C, PDB code: 5cih 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)	35.36 / 2.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.451, 114.219, 88.258, 90.00, 104.32, 90.00
R / Rfree (%)	22.3 / 31

The binding sites of Iron atom in the Complex of Yeast Cytochrome C Peroxidase (W191Y) with Iso-1 Cytochrome C (pdb code 5cih). 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 (W191Y) with Iso-1 Cytochrome C, PDB code: 5cih:
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 (W191Y) 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 (W191Y) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:45.4 occ:1.00 FE A:HEM301 0.0 45.4 1.0 NB A:HEM301 2.0 43.7 1.0 NE2 A:HIS175 2.0 30.0 1.0 NC A:HEM301 2.1 36.6 1.0 ND A:HEM301 2.1 40.6 1.0 NA A:HEM301 2.1 43.5 1.0 CE1 A:HIS175 3.0 42.2 1.0 C1B A:HEM301 3.0 49.0 1.0 CD2 A:HIS175 3.0 35.2 1.0 C4C A:HEM301 3.0 38.1 1.0 C1D A:HEM301 3.1 46.5 1.0 C4A A:HEM301 3.1 37.2 1.0 C1A A:HEM301 3.1 38.0 1.0 C4D A:HEM301 3.1 36.4 1.0 C4B A:HEM301 3.1 51.4 1.0 C1C A:HEM301 3.1 39.0 1.0 CHD A:HEM301 3.4 47.5 1.0 CHB A:HEM301 3.4 44.9 1.0 CHA A:HEM301 3.4 38.1 1.0 CHC A:HEM301 3.5 41.3 1.0 ND1 A:HIS175 4.1 50.1 1.0 CG A:HIS175 4.2 47.5 1.0 C2B A:HEM301 4.2 44.3 1.0 C3A A:HEM301 4.3 50.5 1.0 C2A A:HEM301 4.3 47.4 1.0 C3C A:HEM301 4.3 44.4 1.0 C2D A:HEM301 4.3 42.9 1.0 C3B A:HEM301 4.3 45.4 1.0 C2C A:HEM301 4.3 34.1 1.0 C3D A:HEM301 4.3 42.6 1.0 OH A:TYR191 4.6 62.1 1.0 NE1 A:TRP51 4.6 40.9 1.0 NH1 A:ARG48 4.8 78.4 1.0 CD A:ARG48 4.9 42.7 1.0 CD1 A:TRP51 4.9 40.7 1.0

Iron binding site 2 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191Y) 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 (W191Y) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:67.7 occ:1.00 FE B:HEM201 0.0 67.7 1.0 NE2 B:HIS18 2.0 56.9 1.0 NA B:HEM201 2.0 84.0 1.0 NC B:HEM201 2.1 71.1 1.0 NB B:HEM201 2.1 75.7 1.0 ND B:HEM201 2.1 70.3 1.0 SD B:MET80 2.3 70.2 1.0 CE1 B:HIS18 3.0 63.4 1.0 CD2 B:HIS18 3.0 52.0 1.0 C1A B:HEM201 3.1 80.3 1.0 C4A B:HEM201 3.1 77.4 1.0 C4C B:HEM201 3.1 59.2 1.0 C1D B:HEM201 3.1 64.1 1.0 C1B B:HEM201 3.1 78.5 1.0 C4D B:HEM201 3.1 72.6 1.0 C1C B:HEM201 3.1 70.0 1.0 C4B B:HEM201 3.1 74.7 1.0 CE B:MET80 3.2 47.3 1.0 CG B:MET80 3.3 50.4 1.0 CHD B:HEM201 3.4 57.3 1.0 CHA B:HEM201 3.4 76.7 1.0 CHB B:HEM201 3.4 73.1 1.0 CHC B:HEM201 3.4 76.7 1.0 ND1 B:HIS18 4.1 62.1 1.0 CG B:HIS18 4.1 57.0 1.0 CB B:MET80 4.2 62.6 1.0 C2A B:HEM201 4.3 67.3 1.0 C3A B:HEM201 4.3 68.3 1.0 C3C B:HEM201 4.3 62.2 1.0 C2B B:HEM201 4.3 79.6 1.0 C2C B:HEM201 4.3 62.5 1.0 C2D B:HEM201 4.3 68.1 1.0 C3B B:HEM201 4.3 73.1 1.0 C3D B:HEM201 4.3 75.1 1.0

Iron binding site 3 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191Y) 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 (W191Y) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:55.6 occ:1.00 FE C:HEM301 0.0 55.6 1.0 NA C:HEM301 2.0 60.4 1.0 NE2 C:HIS175 2.0 26.4 1.0 NB C:HEM301 2.1 50.4 1.0 NC C:HEM301 2.1 50.6 1.0 ND C:HEM301 2.1 46.2 1.0 CE1 C:HIS175 3.0 48.0 1.0 CD2 C:HIS175 3.0 35.8 1.0 C4A C:HEM301 3.0 49.6 1.0 C1B C:HEM301 3.1 47.8 1.0 C1A C:HEM301 3.1 45.4 1.0 C1D C:HEM301 3.1 58.6 1.0 C4C C:HEM301 3.1 47.5 1.0 C4D C:HEM301 3.1 41.1 1.0 C4B C:HEM301 3.1 52.0 1.0 C1C C:HEM301 3.1 44.4 1.0 CHB C:HEM301 3.4 45.4 1.0 CHA C:HEM301 3.4 38.6 1.0 CHD C:HEM301 3.4 58.2 1.0 CHC C:HEM301 3.5 51.2 1.0 ND1 C:HIS175 4.1 60.5 1.0 CG C:HIS175 4.1 51.4 1.0 C3A C:HEM301 4.2 46.3 1.0 C2A C:HEM301 4.3 48.0 1.0 C2B C:HEM301 4.3 53.4 1.0 C3B C:HEM301 4.3 54.3 1.0 C3C C:HEM301 4.3 50.4 1.0 C2D C:HEM301 4.3 45.7 1.0 C2C C:HEM301 4.3 37.5 1.0 C3D C:HEM301 4.3 38.5 1.0 NE1 C:TRP51 4.4 26.7 1.0 NE C:ARG48 4.6 41.2 1.0 OH C:TYR191 4.7 69.3 1.0 CD1 C:TRP51 4.9 41.0 1.0

Iron binding site 4 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191Y) 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 (W191Y) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:0.1 occ:1.00 FE D:HEM201 0.0 0.1 1.0 NE2 D:HIS18 2.0 0.4 1.0 ND D:HEM201 2.0 76.1 1.0 NC D:HEM201 2.1 91.7 1.0 NB D:HEM201 2.1 71.4 1.0 NA D:HEM201 2.1 86.8 1.0 SD D:MET80 2.3 93.0 1.0 CE D:MET80 2.8 95.5 1.0 CD2 D:HIS18 3.0 0.7 1.0 CE1 D:HIS18 3.0 98.2 1.0 C4D D:HEM201 3.0 80.2 1.0 C1D D:HEM201 3.1 83.0 1.0 C4C D:HEM201 3.1 86.7 1.0 C4A D:HEM201 3.1 89.9 1.0 C1B D:HEM201 3.1 80.0 1.0 C1A D:HEM201 3.1 91.4 1.0 C1C D:HEM201 3.1 86.8 1.0 C4B D:HEM201 3.1 81.0 1.0 CHA D:HEM201 3.4 80.8 1.0 CHD D:HEM201 3.4 80.9 1.0 CHB D:HEM201 3.4 84.3 1.0 CHC D:HEM201 3.5 81.1 1.0 CG D:MET80 3.7 0.5 1.0 ND1 D:HIS18 4.1 94.8 1.0 CG D:HIS18 4.1 96.3 1.0 C3D D:HEM201 4.3 89.0 1.0 C3A D:HEM201 4.3 98.5 1.0 C2D D:HEM201 4.3 81.3 1.0 C3C D:HEM201 4.3 84.7 1.0 C2B D:HEM201 4.3 80.7 1.0 C2A D:HEM201 4.3 96.9 1.0 C2C D:HEM201 4.3 82.8 1.0 C3B D:HEM201 4.3 82.4 1.0 CB D:MET80 4.7 0.0 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