Iron in PDB 6p42: Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex with Iso-1 Cytochrome C

All present enzymatic activity of Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex with Iso-1 Cytochrome C:
1.11.1.5;

The structure of Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex with Iso-1 Cytochrome C, PDB code: 6p42 was solved by E.F.Yee, B.R.Crane, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.82 / 2.91
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.926, 111.918, 88.747, 90.00, 105.63, 90.00
R / Rfree (%)	21.2 / 27.1

The binding sites of Iron atom in the Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex with Iso-1 Cytochrome C (pdb code 6p42). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex with Iso-1 Cytochrome C, PDB code: 6p42:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex 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 Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:62.5 occ:1.00 FE A:HEM301 0.0 62.5 1.0 NB A:HEM301 2.0 66.3 1.0 NA A:HEM301 2.0 66.6 1.0 NE2 A:HIS175 2.0 60.2 1.0 NC A:HEM301 2.0 60.4 1.0 ND A:HEM301 2.1 68.3 1.0 CE1 A:HIS175 2.9 57.3 1.0 C4B A:HEM301 3.0 65.8 1.0 C1C A:HEM301 3.0 62.3 1.0 C4A A:HEM301 3.0 69.7 1.0 C1B A:HEM301 3.1 63.5 1.0 C1A A:HEM301 3.1 64.0 1.0 C4C A:HEM301 3.1 61.1 1.0 C1D A:HEM301 3.1 60.9 1.0 C4D A:HEM301 3.1 60.8 1.0 CD2 A:HIS175 3.1 67.6 1.0 CHC A:HEM301 3.4 66.0 1.0 CHB A:HEM301 3.4 66.6 1.0 CHD A:HEM301 3.4 61.9 1.0 CHA A:HEM301 3.4 63.8 1.0 CZ3 A:TRP51 3.5 67.8 1.0 CE3 A:TRP51 4.0 54.0 1.0 ND1 A:HIS175 4.0 58.9 1.0 NH1 A:ARG48 4.1 62.8 1.0 CG A:HIS175 4.2 61.4 1.0 C2C A:HEM301 4.2 57.4 1.0 C3B A:HEM301 4.2 59.4 1.0 C3A A:HEM301 4.3 69.3 1.0 C3C A:HEM301 4.3 55.6 1.0 C2B A:HEM301 4.3 58.3 1.0 C2A A:HEM301 4.3 62.0 1.0 C2D A:HEM301 4.3 57.3 1.0 C3D A:HEM301 4.3 54.9 1.0 CH2 A:TRP51 4.3 72.0 1.0 OH A:TYR191 4.7 63.6 1.0 CG A:ARG48 5.0 55.4 1.0

Iron binding site 2 out of 4 in the Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex 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 Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:64.1 occ:1.00 FE B:HEM201 0.0 64.1 1.0 NE2 B:HIS18 2.0 77.3 1.0 NB B:HEM201 2.0 72.5 1.0 NC B:HEM201 2.0 69.8 1.0 NA B:HEM201 2.1 78.3 1.0 ND B:HEM201 2.1 75.7 1.0 SD B:MET80 2.2 69.3 1.0 CD2 B:HIS18 2.9 69.7 1.0 C1B B:HEM201 3.0 75.4 1.0 C4A B:HEM201 3.0 78.8 1.0 C1C B:HEM201 3.0 72.3 1.0 C4B B:HEM201 3.0 69.7 1.0 CE1 B:HIS18 3.1 73.1 1.0 C1A B:HEM201 3.1 77.7 1.0 C4C B:HEM201 3.1 69.4 1.0 C4D B:HEM201 3.1 77.2 1.0 C1D B:HEM201 3.1 73.4 1.0 CE B:MET80 3.2 73.2 1.0 CG B:MET80 3.3 77.9 1.0 CHB B:HEM201 3.4 73.7 1.0 CHC B:HEM201 3.4 72.6 1.0 CHD B:HEM201 3.5 71.5 1.0 CHA B:HEM201 3.5 69.5 1.0 CG B:HIS18 4.1 70.0 1.0 ND1 B:HIS18 4.1 71.8 1.0 CB B:MET80 4.2 73.0 1.0 C2B B:HEM201 4.2 77.0 1.0 C3A B:HEM201 4.2 76.6 1.0 C3B B:HEM201 4.2 74.6 1.0 C2A B:HEM201 4.3 75.4 1.0 C2C B:HEM201 4.3 71.2 1.0 C3C B:HEM201 4.3 72.5 1.0 C3D B:HEM201 4.3 78.4 1.0 C2D B:HEM201 4.3 73.8 1.0

Iron binding site 3 out of 4 in the Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex 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 Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:57.4 occ:1.00 FE C:HEM301 0.0 57.4 1.0 NA C:HEM301 2.0 62.3 1.0 NE2 C:HIS175 2.0 54.0 1.0 ND C:HEM301 2.0 57.9 1.0 NB C:HEM301 2.1 58.9 1.0 NC C:HEM301 2.1 53.9 1.0 CD2 C:HIS175 2.9 52.0 1.0 C4B C:HEM301 3.0 62.0 1.0 C4A C:HEM301 3.1 61.6 1.0 C1A C:HEM301 3.1 58.2 1.0 C1D C:HEM301 3.1 54.8 1.0 C1B C:HEM301 3.1 54.7 1.0 C1C C:HEM301 3.1 53.9 1.0 CE1 C:HIS175 3.1 63.4 1.0 C4D C:HEM301 3.1 55.8 1.0 C4C C:HEM301 3.1 56.9 1.0 CHC C:HEM301 3.4 63.9 1.0 CHB C:HEM301 3.4 58.1 1.0 CHA C:HEM301 3.4 55.8 1.0 CHD C:HEM301 3.4 53.6 1.0 CG C:HIS175 4.1 52.3 1.0 NE1 C:TRP51 4.1 55.0 1.0 ND1 C:HIS175 4.1 66.7 1.0 C3B C:HEM301 4.3 52.9 1.0 C3A C:HEM301 4.3 54.6 1.0 C2B C:HEM301 4.3 55.7 1.0 C2A C:HEM301 4.3 58.6 1.0 C2D C:HEM301 4.3 56.9 1.0 C3D C:HEM301 4.3 52.7 1.0 C2C C:HEM301 4.3 56.7 1.0 C3C C:HEM301 4.3 58.9 1.0 CD1 C:TRP51 4.4 57.4 1.0 OH C:TYR191 4.7 66.0 1.0 NE C:ARG48 4.7 59.1 1.0 CD C:ARG48 4.9 53.4 1.0 CG C:ARG48 5.0 52.5 1.0

Iron binding site 4 out of 4 in the Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex 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 Yeast Cytochrome C Peroxidase (W191Y:L232H) in Complex with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:78.3 occ:1.00 FE D:HEM201 0.0 78.3 1.0 NA D:HEM201 2.0 89.7 1.0 NB D:HEM201 2.0 80.0 1.0 NE2 D:HIS18 2.0 81.0 1.0 ND D:HEM201 2.1 86.3 1.0 NC D:HEM201 2.1 88.3 1.0 SD D:MET80 2.2 61.9 1.0 CE1 D:HIS18 2.7 83.2 1.0 C1A D:HEM201 2.9 89.8 1.0 C4A D:HEM201 3.0 89.2 1.0 C4B D:HEM201 3.0 80.4 1.0 C1B D:HEM201 3.0 84.2 1.0 C4D D:HEM201 3.1 82.1 1.0 C1C D:HEM201 3.1 86.6 1.0 C1D D:HEM201 3.1 86.7 1.0 C4C D:HEM201 3.1 72.5 1.0 CD2 D:HIS18 3.2 78.5 1.0 CHB D:HEM201 3.3 89.1 1.0 CHA D:HEM201 3.4 83.5 1.0 CHC D:HEM201 3.4 84.1 1.0 CHD D:HEM201 3.5 78.3 1.0 CG D:MET80 3.5 81.8 1.0 CE D:MET80 3.8 87.8 1.0 ND1 D:HIS18 3.9 82.0 1.0 C2A D:HEM201 4.1 90.5 1.0 C3A D:HEM201 4.1 88.4 1.0 CG D:HIS18 4.2 86.0 1.0 C3B D:HEM201 4.2 76.8 1.0 C2B D:HEM201 4.2 80.3 1.0 C3D D:HEM201 4.3 91.1 1.0 C2D D:HEM201 4.3 88.9 1.0 C2C D:HEM201 4.3 77.0 1.0 C3C D:HEM201 4.3 76.2 1.0 CB D:MET80 4.4 78.7 1.0

E.F.Yee, B.Dzikovski, B.R.Crane. Tuning Radical Relay Residues By Proton Management Rescues Protein Electron Hopping. J.Am.Chem.Soc. V. 141 17571 2019.
ISSN: ESSN 1520-5126
PubMed: 31603693
DOI: 10.1021/JACS.9B05715