Iron in PDB 5cid: Complex of Yeast Cytochrome C Peroxidase (W191G) Bound to O-Toluidine with Iso-1 Cytochrome C

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

The structure of Complex of Yeast Cytochrome C Peroxidase (W191G) Bound to O-Toluidine with Iso-1 Cytochrome C, PDB code: 5cid 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)	42.58 / 2.76
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.380, 111.906, 87.894, 90.00, 104.33, 90.00
R / Rfree (%)	21.4 / 26.8

The binding sites of Iron atom in the Complex of Yeast Cytochrome C Peroxidase (W191G) Bound to O-Toluidine with Iso-1 Cytochrome C (pdb code 5cid). 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) Bound to O-Toluidine with Iso-1 Cytochrome C, PDB code: 5cid:
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) Bound to O-Toluidine 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) Bound to O-Toluidine with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:32.7 occ:1.00 FE A:HEM301 0.0 32.7 1.0 ND A:HEM301 2.0 42.3 1.0 NC A:HEM301 2.0 38.0 1.0 NE2 A:HIS175 2.1 29.6 1.0 NA A:HEM301 2.1 41.9 1.0 NB A:HEM301 2.2 41.6 1.0 C1D A:HEM301 3.0 44.3 1.0 C4D A:HEM301 3.0 42.6 1.0 C4C A:HEM301 3.0 38.6 1.0 CD2 A:HIS175 3.1 36.6 1.0 C1A A:HEM301 3.1 43.0 1.0 CE1 A:HIS175 3.1 35.2 1.0 C1C A:HEM301 3.1 41.3 1.0 C4B A:HEM301 3.1 40.8 1.0 C4A A:HEM301 3.2 50.8 1.0 C1B A:HEM301 3.2 43.5 1.0 CHD A:HEM301 3.4 44.2 1.0 CHA A:HEM301 3.4 48.5 1.0 CHC A:HEM301 3.5 36.1 1.0 CHB A:HEM301 3.6 42.6 1.0 ND1 A:HIS175 4.2 34.6 1.0 CG A:HIS175 4.2 39.4 1.0 C2D A:HEM301 4.2 48.2 1.0 C3D A:HEM301 4.2 47.8 1.0 C3C A:HEM301 4.3 38.1 1.0 C2C A:HEM301 4.3 39.7 1.0 NE1 A:TRP51 4.3 40.6 1.0 C2A A:HEM301 4.3 45.7 1.0 C3A A:HEM301 4.4 51.8 1.0 C3B A:HEM301 4.4 42.7 1.0 C2B A:HEM301 4.4 49.7 1.0 CD1 A:TRP51 4.4 42.7 1.0 NH2 A:51V302 4.6 56.8 1.0

Iron binding site 2 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191G) Bound to O-Toluidine 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) Bound to O-Toluidine with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:67.1 occ:1.00 FE B:HEM201 0.0 67.1 1.0 NE2 B:HIS18 2.0 71.7 1.0 NA B:HEM201 2.0 79.5 1.0 NB B:HEM201 2.1 65.4 1.0 NC B:HEM201 2.1 73.4 1.0 ND B:HEM201 2.1 73.5 1.0 SD B:MET80 2.3 74.3 1.0 CE1 B:HIS18 2.9 72.3 1.0 C4A B:HEM201 3.0 74.2 1.0 C1B B:HEM201 3.0 68.5 1.0 CD2 B:HIS18 3.1 67.4 1.0 C1A B:HEM201 3.1 79.8 1.0 C1D B:HEM201 3.1 70.5 1.0 C4D B:HEM201 3.1 75.9 1.0 C4B B:HEM201 3.1 65.7 1.0 C4C B:HEM201 3.1 68.2 1.0 C1C B:HEM201 3.1 69.1 1.0 CHB B:HEM201 3.4 69.4 1.0 CHD B:HEM201 3.4 64.5 1.0 CHA B:HEM201 3.4 78.8 1.0 CHC B:HEM201 3.5 68.8 1.0 CE B:MET80 3.6 59.4 1.0 CG B:MET80 3.7 68.0 1.0 ND1 B:HIS18 4.1 70.9 1.0 CG B:HIS18 4.2 69.7 1.0 C3A B:HEM201 4.2 78.1 1.0 C2B B:HEM201 4.3 65.0 1.0 C2A B:HEM201 4.3 80.2 1.0 CB B:MET80 4.3 70.1 1.0 C3B B:HEM201 4.3 58.7 1.0 C2D B:HEM201 4.3 77.5 1.0 C3D B:HEM201 4.3 80.7 1.0 C3C B:HEM201 4.3 69.0 1.0 C2C B:HEM201 4.4 67.3 1.0

Iron binding site 3 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191G) Bound to O-Toluidine 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) Bound to O-Toluidine with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:26.1 occ:1.00 FE C:HEM301 0.0 26.1 1.0 NC C:HEM301 2.0 41.7 1.0 NE2 C:HIS175 2.1 34.3 1.0 ND C:HEM301 2.1 40.7 1.0 NA C:HEM301 2.1 45.7 1.0 NB C:HEM301 2.1 38.8 1.0 C4C C:HEM301 3.0 40.5 1.0 C1D C:HEM301 3.0 38.7 1.0 CE1 C:HIS175 3.0 41.9 1.0 CD2 C:HIS175 3.1 41.9 1.0 C1C C:HEM301 3.1 43.0 1.0 C4D C:HEM301 3.1 42.6 1.0 C4B C:HEM301 3.1 41.7 1.0 C1A C:HEM301 3.1 41.0 1.0 C4A C:HEM301 3.1 44.6 1.0 C1B C:HEM301 3.1 34.1 1.0 CHD C:HEM301 3.4 41.0 1.0 CHC C:HEM301 3.4 39.8 1.0 CHA C:HEM301 3.5 46.1 1.0 CHB C:HEM301 3.5 42.1 1.0 ND1 C:HIS175 4.2 44.7 1.0 CG C:HIS175 4.2 41.7 1.0 C3C C:HEM301 4.2 44.3 1.0 NE1 C:TRP51 4.3 40.9 1.0 C2D C:HEM301 4.3 43.2 1.0 C2C C:HEM301 4.3 43.2 1.0 C3D C:HEM301 4.3 44.8 1.0 C3B C:HEM301 4.3 44.9 1.0 C2B C:HEM301 4.3 44.8 1.0 C3A C:HEM301 4.3 42.2 1.0 C2A C:HEM301 4.3 42.6 1.0 CD1 C:TRP51 4.5 44.0 1.0

Iron binding site 4 out of 4 in the Complex of Yeast Cytochrome C Peroxidase (W191G) Bound to O-Toluidine 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) Bound to O-Toluidine with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:0.8 occ:1.00 FE D:HEM201 0.0 0.8 1.0 NE2 D:HIS18 2.0 0.2 1.0 NC D:HEM201 2.0 0.3 1.0 ND D:HEM201 2.1 0.6 1.0 NA D:HEM201 2.1 0.2 1.0 NB D:HEM201 2.1 0.8 1.0 SD D:MET80 2.2 0.4 1.0 CE1 D:HIS18 2.8 0.5 1.0 C4C D:HEM201 3.0 0.9 1.0 C1D D:HEM201 3.0 0.7 1.0 C1C D:HEM201 3.1 0.3 1.0 C4D D:HEM201 3.1 1.0 1.0 C4B D:HEM201 3.1 0.4 1.0 C1A D:HEM201 3.1 0.8 1.0 C4A D:HEM201 3.1 0.3 1.0 CD2 D:HIS18 3.1 0.8 1.0 C1B D:HEM201 3.1 0.8 1.0 CHD D:HEM201 3.3 0.3 1.0 CHC D:HEM201 3.4 0.5 1.0 CHA D:HEM201 3.4 0.1 1.0 CE D:MET80 3.5 0.8 1.0 CHB D:HEM201 3.5 0.8 1.0 CG D:MET80 3.6 0.8 1.0 ND1 D:HIS18 4.0 0.1 1.0 NZ D:LYS27 4.2 0.8 1.0 CG D:HIS18 4.2 0.7 1.0 CB D:MET80 4.2 0.8 1.0 C3C D:HEM201 4.2 0.4 1.0 C2C D:HEM201 4.3 0.7 1.0 C2D D:HEM201 4.3 0.8 1.0 C3D D:HEM201 4.3 0.1 1.0 C3B D:HEM201 4.3 96.4 1.0 C2A D:HEM201 4.3 0.2 1.0 C3A D:HEM201 4.3 1.0 1.0 C2B D:HEM201 4.3 95.4 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