Iron in PDB 6p41: Yeast Cytochrome C Peroxidase (W191Y:L232E) in Complex with Iso-1 Cytochrome C

All present enzymatic activity of Yeast Cytochrome C Peroxidase (W191Y:L232E) in Complex with Iso-1 Cytochrome C:
1.11.1.5;

The structure of Yeast Cytochrome C Peroxidase (W191Y:L232E) in Complex with Iso-1 Cytochrome C, PDB code: 6p41 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)	44.32 / 2.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.803, 112.070, 88.327, 90.00, 104.64, 90.00
R / Rfree (%)	23.7 / 27.3

The binding sites of Iron atom in the Yeast Cytochrome C Peroxidase (W191Y:L232E) in Complex with Iso-1 Cytochrome C (pdb code 6p41). 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:L232E) in Complex with Iso-1 Cytochrome C, PDB code: 6p41:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Yeast Cytochrome C Peroxidase (W191Y:L232E) 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:L232E) in Complex with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:73.2 occ:1.00 FE A:HEM301 0.0 73.2 1.0 NE2 A:HIS175 2.0 70.7 1.0 ND A:HEM301 2.0 84.5 1.0 NB A:HEM301 2.1 87.9 1.0 NA A:HEM301 2.1 78.4 1.0 NC A:HEM301 2.1 82.2 1.0 CD2 A:HIS175 2.8 73.3 1.0 C1C A:HEM301 3.0 76.9 1.0 C4C A:HEM301 3.0 76.8 1.0 C4D A:HEM301 3.1 76.7 1.0 C1D A:HEM301 3.1 78.7 1.0 C4B A:HEM301 3.1 82.7 1.0 C1B A:HEM301 3.1 83.2 1.0 C4A A:HEM301 3.1 80.8 1.0 C1A A:HEM301 3.1 88.2 1.0 CE1 A:HIS175 3.2 78.1 1.0 CHC A:HEM301 3.4 82.6 1.0 CHD A:HEM301 3.4 75.2 1.0 CHA A:HEM301 3.4 79.5 1.0 CHB A:HEM301 3.4 85.5 1.0 CG A:HIS175 4.0 72.5 1.0 ND1 A:HIS175 4.2 75.6 1.0 C2C A:HEM301 4.2 70.7 1.0 C3C A:HEM301 4.2 70.5 1.0 C3D A:HEM301 4.3 71.7 1.0 C2D A:HEM301 4.3 72.8 1.0 CD1 A:TRP51 4.3 72.8 1.0 C2B A:HEM301 4.3 76.9 1.0 C3B A:HEM301 4.3 77.3 1.0 C3A A:HEM301 4.3 78.0 1.0 C2A A:HEM301 4.3 78.6 1.0 NE1 A:TRP51 4.3 73.9 1.0 CG A:ARG48 4.9 70.5 1.0 NE2 A:HIS52 4.9 79.4 1.0

Iron binding site 2 out of 4 in the Yeast Cytochrome C Peroxidase (W191Y:L232E) 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:L232E) in Complex with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:94.2 occ:1.00 FE B:HEM201 0.0 94.2 1.0 NE2 B:HIS18 2.0 86.0 1.0 NB B:HEM201 2.0 90.2 1.0 NC B:HEM201 2.0 87.3 1.0 NA B:HEM201 2.0 0.4 1.0 ND B:HEM201 2.1 92.2 1.0 SD B:MET80 2.2 87.9 1.0 CE1 B:HIS18 2.4 85.5 1.0 C1D B:HEM201 3.0 87.5 1.0 C1B B:HEM201 3.0 95.5 1.0 C4C B:HEM201 3.0 84.5 1.0 C4A B:HEM201 3.0 99.4 1.0 C4B B:HEM201 3.1 85.2 1.0 C4D B:HEM201 3.1 93.3 1.0 C1C B:HEM201 3.1 86.0 1.0 C1A B:HEM201 3.1 0.5 1.0 CD2 B:HIS18 3.3 83.2 1.0 CHD B:HEM201 3.4 85.8 1.0 CHB B:HEM201 3.4 94.8 1.0 CG B:MET80 3.4 86.6 1.0 CHC B:HEM201 3.4 79.4 1.0 CHA B:HEM201 3.5 0.7 1.0 ND1 B:HIS18 3.6 81.4 1.0 CE B:MET80 3.8 89.7 1.0 CB B:MET80 4.1 88.1 1.0 CG B:HIS18 4.1 81.5 1.0 C2D B:HEM201 4.2 88.7 1.0 C3D B:HEM201 4.2 92.1 1.0 C2B B:HEM201 4.3 94.3 1.0 C3A B:HEM201 4.3 0.8 1.0 C3B B:HEM201 4.3 92.5 1.0 C3C B:HEM201 4.3 84.3 1.0 C2C B:HEM201 4.3 83.0 1.0 C2A B:HEM201 4.3 0.4 1.0 OH B:TYR67 4.9 82.7 1.0 CD1 B:LEU32 4.9 93.8 1.0 CD B:PRO30 4.9 89.1 1.0

Iron binding site 3 out of 4 in the Yeast Cytochrome C Peroxidase (W191Y:L232E) 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:L232E) in Complex with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:81.2 occ:1.00 FE C:HEM301 0.0 81.2 1.0 ND C:HEM301 2.0 73.9 1.0 NE2 C:HIS175 2.0 76.0 1.0 NC C:HEM301 2.0 74.9 1.0 NA C:HEM301 2.1 81.2 1.0 NB C:HEM301 2.1 81.1 1.0 CE1 C:HIS175 2.9 80.5 1.0 CD2 C:HIS175 3.0 73.6 1.0 C4C C:HEM301 3.0 75.4 1.0 C1D C:HEM301 3.0 76.4 1.0 C1C C:HEM301 3.0 76.0 1.0 C4D C:HEM301 3.0 79.8 1.0 C1A C:HEM301 3.1 76.1 1.0 C4B C:HEM301 3.1 72.2 1.0 C4A C:HEM301 3.1 81.0 1.0 C1B C:HEM301 3.1 73.2 1.0 CHD C:HEM301 3.4 73.5 1.0 CHA C:HEM301 3.4 82.0 1.0 CHC C:HEM301 3.4 74.3 1.0 CHB C:HEM301 3.5 74.0 1.0 NE1 C:TRP51 3.7 70.6 1.0 ND1 C:HIS175 3.9 82.2 1.0 CG C:HIS175 4.0 73.5 1.0 C3C C:HEM301 4.2 70.0 1.0 C2C C:HEM301 4.2 69.8 1.0 C2D C:HEM301 4.2 77.1 1.0 C3D C:HEM301 4.2 67.9 1.0 C2A C:HEM301 4.3 73.6 1.0 C3A C:HEM301 4.3 79.1 1.0 C3B C:HEM301 4.3 76.2 1.0 C2B C:HEM301 4.3 80.2 1.0 CD1 C:TRP51 4.4 68.1 1.0 CE2 C:TRP51 4.6 73.6 1.0 NE2 C:HIS52 5.0 68.9 1.0 CZ2 C:TRP51 5.0 70.6 1.0

Iron binding site 4 out of 4 in the Yeast Cytochrome C Peroxidase (W191Y:L232E) 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:L232E) in Complex with Iso-1 Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:1.0 occ:1.00 FE D:HEM201 0.0 1.0 1.0 NE2 D:HIS18 2.0 0.9 1.0 NB D:HEM201 2.0 0.7 1.0 NA D:HEM201 2.0 0.2 1.0 NC D:HEM201 2.0 0.1 1.0 ND D:HEM201 2.1 0.1 1.0 CE1 D:HIS18 2.2 0.3 1.0 SD D:MET80 2.3 0.6 1.0 C4B D:HEM201 3.0 0.7 1.0 C4D D:HEM201 3.0 1.0 1.0 C1A D:HEM201 3.1 0.2 1.0 C1C D:HEM201 3.1 0.8 1.0 C1B D:HEM201 3.1 0.4 1.0 C1D D:HEM201 3.1 0.3 1.0 C4A D:HEM201 3.1 0.3 1.0 C4C D:HEM201 3.1 0.7 1.0 CG D:MET80 3.3 0.2 1.0 CD2 D:HIS18 3.3 0.0 1.0 CHC D:HEM201 3.4 0.9 1.0 CHA D:HEM201 3.4 0.9 1.0 CHB D:HEM201 3.4 0.4 1.0 CHD D:HEM201 3.4 0.3 1.0 ND1 D:HIS18 3.5 0.7 1.0 CE D:MET80 3.7 0.1 1.0 CB D:MET80 4.0 0.3 1.0 CG D:HIS18 4.1 1.0 1.0 C3D D:HEM201 4.3 0.5 1.0 C2D D:HEM201 4.3 0.5 1.0 C3B D:HEM201 4.3 0.9 1.0 C2B D:HEM201 4.3 0.6 1.0 C2A D:HEM201 4.3 0.6 1.0 C3A D:HEM201 4.3 0.9 1.0 C2C D:HEM201 4.3 0.6 1.0 C3C D:HEM201 4.3 0.1 1.0 OH D:TYR67 4.7 0.8 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