Iron in PDB 1ryc: Cytochrome C Peroxidase W191G From Saccharomyces Cerevisiae

All present enzymatic activity of Cytochrome C Peroxidase W191G From Saccharomyces Cerevisiae:
1.11.1.5;

The structure of Cytochrome C Peroxidase W191G From Saccharomyces Cerevisiae, PDB code: 1ryc was solved by M.M.Fitzgerald, R.Musah, D.E.Mcree, D.B.Goodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	108.000, 77.300, 51.800, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / n/a

The binding sites of Iron atom in the Cytochrome C Peroxidase W191G From Saccharomyces Cerevisiae (pdb code 1ryc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Cytochrome C Peroxidase W191G From Saccharomyces Cerevisiae, PDB code: 1ryc:

Iron binding site 1 out of 1 in the Cytochrome C Peroxidase W191G From Saccharomyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Peroxidase W191G From Saccharomyces Cerevisiae within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe295 b:12.8 occ:1.00 FE A:HEM295 0.0 12.8 1.0 NE2 A:HIS175 2.0 14.8 1.0 O A:HOH313 2.0 16.9 1.0 NA A:HEM295 2.1 13.1 1.0 NB A:HEM295 2.1 13.1 1.0 ND A:HEM295 2.1 12.2 1.0 NC A:HEM295 2.1 13.0 1.0 CE1 A:HIS175 2.8 13.6 1.0 C4A A:HEM295 3.0 13.3 1.0 C1A A:HEM295 3.0 14.8 1.0 C1B A:HEM295 3.0 15.1 1.0 C1D A:HEM295 3.1 12.0 1.0 C4D A:HEM295 3.1 11.9 1.0 CD2 A:HIS175 3.1 15.5 1.0 C4C A:HEM295 3.1 11.6 1.0 C1C A:HEM295 3.1 13.1 1.0 C4B A:HEM295 3.1 13.4 1.0 CHB A:HEM295 3.3 13.7 1.0 CHA A:HEM295 3.4 10.3 1.0 CHD A:HEM295 3.4 9.0 1.0 CHC A:HEM295 3.4 10.2 1.0 ND1 A:HIS175 4.0 13.1 1.0 CG A:HIS175 4.2 13.6 1.0 NE1 A:TRP51 4.2 13.3 1.0 C3A A:HEM295 4.2 13.2 1.0 C2A A:HEM295 4.2 14.3 1.0 C2D A:HEM295 4.3 9.6 1.0 C2B A:HEM295 4.3 14.7 1.0 O A:HOH344 4.3 25.5 1.0 C3D A:HEM295 4.3 9.7 1.0 C3B A:HEM295 4.3 14.3 1.0 C3C A:HEM295 4.3 12.5 1.0 C2C A:HEM295 4.3 12.1 1.0 O A:HOH300 4.3 29.6 1.0 CD1 A:TRP51 4.5 12.6 1.0

M.M.Fitzgerald, R.A.Musah, D.E.Mcree, D.B.Goodin. A Ligand-Gated, Hinged Loop Rearrangement Opens A Channel to A Buried Artificial Protein Cavity. Nat.Struct.Biol. V. 3 626 1996.
ISSN: ISSN 1072-8368
PubMed: 8673607
DOI: 10.1038/NSB0796-626