Iron in PDB 5cig: Complex of Yeast Cytochrome C Peroxidase (W191G) with Iso-1 Cytochrome C

All present enzymatic activity of Complex of Yeast Cytochrome C Peroxidase (W191G) with Iso-1 Cytochrome C:
1.11.1.5;

The structure of Complex of Yeast Cytochrome C Peroxidase (W191G) with Iso-1 Cytochrome C, PDB code: 5cig 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)	29.18 / 2.06
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.380, 117.109, 88.929, 90.00, 105.06, 90.00
R / Rfree (%)	28.2 / 29.8

The binding sites of Iron atom in the Complex of Yeast Cytochrome C Peroxidase (W191G) with Iso-1 Cytochrome C (pdb code 5cig). 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 (W191G) with Iso-1 Cytochrome C, PDB code: 5cig:
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 (W191G) 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 (W191G) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:41.4 occ:1.00 FE A:HEM301 0.0 41.4 1.0 NE2 A:HIS175 2.0 34.9 1.0 NC A:HEM301 2.1 30.5 1.0 NA A:HEM301 2.1 40.4 1.0 NB A:HEM301 2.1 35.4 1.0 ND A:HEM301 2.1 32.3 1.0 CD2 A:HIS175 3.0 33.9 1.0 C4C A:HEM301 3.1 30.9 1.0 C1D A:HEM301 3.1 34.9 1.0 C1B A:HEM301 3.1 38.8 1.0 C4D A:HEM301 3.1 35.5 1.0 C1C A:HEM301 3.1 32.2 1.0 C4A A:HEM301 3.1 36.2 1.0 C4B A:HEM301 3.1 35.1 1.0 CE1 A:HIS175 3.1 35.8 1.0 C1A A:HEM301 3.1 38.8 1.0 CHD A:HEM301 3.4 32.6 1.0 CHA A:HEM301 3.5 35.8 1.0 CHB A:HEM301 3.5 38.2 1.0 CHC A:HEM301 3.5 32.7 1.0 CG A:HIS175 4.1 34.8 1.0 O A:HOH521 4.2 56.9 1.0 ND1 A:HIS175 4.2 37.5 1.0 NE1 A:TRP51 4.2 34.4 1.0 C2D A:HEM301 4.3 34.9 1.0 C2B A:HEM301 4.3 36.4 1.0 C3D A:HEM301 4.3 36.7 1.0 C3C A:HEM301 4.3 34.8 1.0 C3B A:HEM301 4.3 38.0 1.0 C2C A:HEM301 4.3 32.3 1.0 C3A A:HEM301 4.3 38.9 1.0 C2A A:HEM301 4.3 40.4 1.0 CD1 A:TRP51 4.5 35.1 1.0

Iron binding site 2 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191G) 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 (W191G) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:39.9 occ:1.00 FE B:HEM201 0.0 39.9 1.0 NE2 B:HIS18 2.0 38.4 1.0 NA B:HEM201 2.0 36.9 1.0 NB B:HEM201 2.0 34.0 1.0 NC B:HEM201 2.0 37.9 1.0 ND B:HEM201 2.1 40.8 1.0 SD B:MET80 2.3 38.6 1.0 CE1 B:HIS18 2.7 41.4 1.0 C1D B:HEM201 3.0 42.1 1.0 C4C B:HEM201 3.0 37.4 1.0 C1A B:HEM201 3.1 40.4 1.0 C4A B:HEM201 3.1 40.0 1.0 C1B B:HEM201 3.1 41.6 1.0 C4D B:HEM201 3.1 38.7 1.0 C4B B:HEM201 3.1 38.5 1.0 C1C B:HEM201 3.1 34.8 1.0 CD2 B:HIS18 3.2 37.2 1.0 CG B:MET80 3.3 34.7 1.0 CHD B:HEM201 3.4 39.1 1.0 CHA B:HEM201 3.4 41.7 1.0 CE B:MET80 3.4 37.9 1.0 CHB B:HEM201 3.4 38.0 1.0 CHC B:HEM201 3.4 38.2 1.0 ND1 B:HIS18 3.9 36.5 1.0 CG B:HIS18 4.1 39.8 1.0 C2A B:HEM201 4.3 41.4 1.0 CB B:MET80 4.3 37.9 1.0 C3A B:HEM201 4.3 43.6 1.0 C2D B:HEM201 4.3 39.6 1.0 C2B B:HEM201 4.3 41.7 1.0 C3B B:HEM201 4.3 37.2 1.0 C3D B:HEM201 4.3 40.6 1.0 C3C B:HEM201 4.3 36.3 1.0 C2C B:HEM201 4.3 32.2 1.0 OH B:TYR67 5.0 42.1 1.0

Iron binding site 3 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191G) 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 (W191G) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:32.1 occ:1.00 FE C:HEM301 0.0 32.1 1.0 NC C:HEM301 2.1 30.8 1.0 NE2 C:HIS175 2.1 35.0 1.0 NA C:HEM301 2.1 29.1 1.0 NB C:HEM301 2.1 33.0 1.0 ND C:HEM301 2.2 26.4 1.0 CD2 C:HIS175 2.8 35.2 1.0 C4B C:HEM301 3.1 36.0 1.0 C1C C:HEM301 3.1 37.1 1.0 C1B C:HEM301 3.1 34.4 1.0 C4C C:HEM301 3.1 34.3 1.0 C4A C:HEM301 3.1 31.7 1.0 C1D C:HEM301 3.1 31.9 1.0 O C:HOH449 3.1 35.4 1.0 C1A C:HEM301 3.1 34.6 1.0 C4D C:HEM301 3.1 34.5 1.0 CE1 C:HIS175 3.1 38.3 1.0 CHC C:HEM301 3.4 33.4 1.0 CHA C:HEM301 3.5 32.1 1.0 CHD C:HEM301 3.5 25.5 1.0 CHB C:HEM301 3.5 33.3 1.0 CG C:HIS175 4.0 31.8 1.0 ND1 C:HIS175 4.1 33.6 1.0 NE1 C:TRP51 4.2 32.7 1.0 C3B C:HEM301 4.3 31.7 1.0 C2B C:HEM301 4.3 32.0 1.0 C2D C:HEM301 4.3 31.6 1.0 C2C C:HEM301 4.3 33.4 1.0 C3D C:HEM301 4.3 28.6 1.0 C3A C:HEM301 4.3 30.6 1.0 C3C C:HEM301 4.3 30.8 1.0 C2A C:HEM301 4.3 30.4 1.0 CD1 C:TRP51 4.6 33.1 1.0

Iron binding site 4 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191G) 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 (W191G) with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:41.1 occ:1.00 FE D:HEM201 0.0 41.1 1.0 NE2 D:HIS18 2.0 43.9 1.0 NB D:HEM201 2.1 47.3 1.0 NA D:HEM201 2.1 50.4 1.0 ND D:HEM201 2.1 51.9 1.0 NC D:HEM201 2.1 42.9 1.0 SD D:MET80 2.2 48.0 1.0 CE1 D:HIS18 2.9 49.8 1.0 CD2 D:HIS18 3.0 46.2 1.0 O D:HOH302 3.0 54.7 1.0 C4A D:HEM201 3.1 48.9 1.0 C1A D:HEM201 3.1 52.2 1.0 C1D D:HEM201 3.1 51.0 1.0 C4D D:HEM201 3.1 53.5 1.0 C4B D:HEM201 3.1 42.3 1.0 C1B D:HEM201 3.1 44.1 1.0 C4C D:HEM201 3.1 44.8 1.0 C1C D:HEM201 3.1 44.2 1.0 CHB D:HEM201 3.4 44.1 1.0 CHA D:HEM201 3.4 52.8 1.0 CHD D:HEM201 3.4 47.5 1.0 CHC D:HEM201 3.4 41.1 1.0 CE D:MET80 3.5 45.6 1.0 CG D:MET80 3.5 47.0 1.0 ND1 D:HIS18 4.0 49.0 1.0 CG D:HIS18 4.1 50.4 1.0 CB D:MET80 4.2 48.9 1.0 C3A D:HEM201 4.2 50.5 1.0 C2A D:HEM201 4.3 52.6 1.0 C2D D:HEM201 4.3 52.2 1.0 C3D D:HEM201 4.3 54.8 1.0 C3B D:HEM201 4.3 41.6 1.0 C2B D:HEM201 4.3 43.4 1.0 C3C D:HEM201 4.3 46.2 1.0 C2C D:HEM201 4.3 42.8 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